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LitCovid-PubTator

LitCovid-PD-FMA-UBERON

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T178","span":{"begin":135,"end":142},"obj":"Body_part"},{"id":"T179","span":{"begin":350,"end":359},"obj":"Body_part"},{"id":"T180","span":{"begin":1336,"end":1340},"obj":"Body_part"}],"attributes":[{"id":"A178","pred":"fma_id","subj":"T178","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A179","pred":"fma_id","subj":"T179","obj":"http://purl.org/sig/ont/fma/fma84050"},{"id":"A180","pred":"fma_id","subj":"T180","obj":"http://purl.org/sig/ont/fma/fma256135"}],"text":"Molecular interactions and binding conformation of the designed MEPVC with TLR3 and TLR4 innate immune receptors were deciphered via a protein-peptide docking approach. Both TLR3 and TLR4 belong to toll-like receptor family of pattern recognition receptor and function to activate intracellular signaling NF-κB pathway and production of inflammatory cytokines responsible for the development of effective innate immunity [79,80]. These receptors recognize viral associated molecular patterns and induce the production of interferon leading to activation of strong host defense responses. Also, the specific adaptive immunity takes time to establish against antigens therefore it's important to evaluate MEPVC affinity for the innate immune receptors. In case of MRPVC-TLR3 complex, the patch dock predicted 10 best solutions sorted based on the docking geometric shape complementarity score (S-Table 3). A high score implies enhanced affinity of the interacting molecules and best docked conformations of the molecules with respect to each other. Solution 3 was visualized for docked conformations and intermolecular forces responsible for such high affinity of the molecules. The selection was based on the FireDock analysis (S-Table 4) which is an efficient package for refinement and reassigning procedure of docking scores to rigid body docking solutions. The global binding energy of solution 3 is better i.e. -6.39 kJ/mol compared to the rest of predicted solutions. The contribution to the total score form attractive van der Waals (VdW) energy is -12.12 kJ/mol, repulsive (VdW) energy (4.79 kJ/mol), hydrogen bond (HB) energy (-1.63 kJ/mol), and atomic contact energy (ACE) (5.95 kJ/mol). The MEPVC, within 3 Å, was noticed to posed right in the center of the TLR3 receptor (Figure 7 ) interacting via hydrogen and hydrophobic bonds with His156, Asp180, Lys201, Glu203, Ser206, Phe227, Asp229, Asp230, Ser254, Ser256, Asp257, Ser282, Tyr283, Asp284, Asp285, Glu301, Tyr302, Phe304, Glu306, Tyr307, Arg325, Glu358, His359, Lys382, Tyr383, P408, His410, Iso411, Gly431, His432, Glu434, Pro408, Asp457, Phe459, Gln483, and Glu533. Similarly, among 10 predicted MEPVC-TLR4 complexes (S-Table 5), solution 7 (S-Table 6) was affirmed as best with total global energy of -10.39 kJ/mol whereas the rest of complexes were noticed as highly unstable with score in positive. The attractive VdW, repulsive VdW, HB and ACE contribution to the global energy is -35.75 kJ/mol, 22.04 kJ/mol, -5.51 kJ/mol, and 12.61 kJ/mol, respectively. Visual analysis of the complex revealed binding of the MEPVC at the interface of chains B and D (Figure 8 ). The MEPVC is surrounded by chain B residues: Pro23, Glu24, Ser25, Asp44, Lys47, Asp50, Asp51, Arg67, Arg87, Glu89, Pro113, Gln115, Asp137, His159, Asp160, Ser184, and Lys186 and chain D residues: Lys20, Phe64, and Asp114.\nFig. 7 Binding conformation of MEPVC with respect to TLR3 innate immune receptor. The yellow labeled region pointing to the residues involved in both hydrophobic and hydrophilic interactions with MEPVC.\nFig. 8 Binding conformation of MEPVC with respect to TLR4 innate immune receptor. The yellow labeled region pointing to the residues involved in both hydrophobic and hydrophilic interactions with MEPVC."}

LitCovid-PD-CLO

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T253","span":{"begin":133,"end":134},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T254","span":{"begin":143,"end":150},"obj":"http://purl.obolibrary.org/obo/PR_000018263"},{"id":"T255","span":{"begin":272,"end":280},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"},{"id":"T256","span":{"begin":295,"end":304},"obj":"http://purl.obolibrary.org/obo/SO_0000418"},{"id":"T257","span":{"begin":309,"end":310},"obj":"http://purl.obolibrary.org/obo/CLO_0001021"},{"id":"T258","span":{"begin":543,"end":553},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"},{"id":"T259","span":{"begin":904,"end":905},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T260","span":{"begin":1623,"end":1625},"obj":"http://purl.obolibrary.org/obo/CLO_0003622"},{"id":"T261","span":{"begin":1717,"end":1718},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T262","span":{"begin":2407,"end":2409},"obj":"http://purl.obolibrary.org/obo/CLO_0003622"},{"id":"T263","span":{"begin":2618,"end":2619},"obj":"http://purl.obolibrary.org/obo/CLO_0001021"},{"id":"T264","span":{"begin":2672,"end":2673},"obj":"http://purl.obolibrary.org/obo/CLO_0001021"},{"id":"T265","span":{"begin":2954,"end":2961},"obj":"http://purl.obolibrary.org/obo/CLO_0007225"},{"id":"T266","span":{"begin":3157,"end":3164},"obj":"http://purl.obolibrary.org/obo/CLO_0007225"}],"text":"Molecular interactions and binding conformation of the designed MEPVC with TLR3 and TLR4 innate immune receptors were deciphered via a protein-peptide docking approach. Both TLR3 and TLR4 belong to toll-like receptor family of pattern recognition receptor and function to activate intracellular signaling NF-κB pathway and production of inflammatory cytokines responsible for the development of effective innate immunity [79,80]. These receptors recognize viral associated molecular patterns and induce the production of interferon leading to activation of strong host defense responses. Also, the specific adaptive immunity takes time to establish against antigens therefore it's important to evaluate MEPVC affinity for the innate immune receptors. In case of MRPVC-TLR3 complex, the patch dock predicted 10 best solutions sorted based on the docking geometric shape complementarity score (S-Table 3). A high score implies enhanced affinity of the interacting molecules and best docked conformations of the molecules with respect to each other. Solution 3 was visualized for docked conformations and intermolecular forces responsible for such high affinity of the molecules. The selection was based on the FireDock analysis (S-Table 4) which is an efficient package for refinement and reassigning procedure of docking scores to rigid body docking solutions. The global binding energy of solution 3 is better i.e. -6.39 kJ/mol compared to the rest of predicted solutions. The contribution to the total score form attractive van der Waals (VdW) energy is -12.12 kJ/mol, repulsive (VdW) energy (4.79 kJ/mol), hydrogen bond (HB) energy (-1.63 kJ/mol), and atomic contact energy (ACE) (5.95 kJ/mol). The MEPVC, within 3 Å, was noticed to posed right in the center of the TLR3 receptor (Figure 7 ) interacting via hydrogen and hydrophobic bonds with His156, Asp180, Lys201, Glu203, Ser206, Phe227, Asp229, Asp230, Ser254, Ser256, Asp257, Ser282, Tyr283, Asp284, Asp285, Glu301, Tyr302, Phe304, Glu306, Tyr307, Arg325, Glu358, His359, Lys382, Tyr383, P408, His410, Iso411, Gly431, His432, Glu434, Pro408, Asp457, Phe459, Gln483, and Glu533. Similarly, among 10 predicted MEPVC-TLR4 complexes (S-Table 5), solution 7 (S-Table 6) was affirmed as best with total global energy of -10.39 kJ/mol whereas the rest of complexes were noticed as highly unstable with score in positive. The attractive VdW, repulsive VdW, HB and ACE contribution to the global energy is -35.75 kJ/mol, 22.04 kJ/mol, -5.51 kJ/mol, and 12.61 kJ/mol, respectively. Visual analysis of the complex revealed binding of the MEPVC at the interface of chains B and D (Figure 8 ). The MEPVC is surrounded by chain B residues: Pro23, Glu24, Ser25, Asp44, Lys47, Asp50, Asp51, Arg67, Arg87, Glu89, Pro113, Gln115, Asp137, His159, Asp160, Ser184, and Lys186 and chain D residues: Lys20, Phe64, and Asp114.\nFig. 7 Binding conformation of MEPVC with respect to TLR3 innate immune receptor. The yellow labeled region pointing to the residues involved in both hydrophobic and hydrophilic interactions with MEPVC.\nFig. 8 Binding conformation of MEPVC with respect to TLR4 innate immune receptor. The yellow labeled region pointing to the residues involved in both hydrophobic and hydrophilic interactions with MEPVC."}

LitCovid-PD-CHEBI

LitCovid-PD-GO-BP

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T47","span":{"begin":89,"end":102},"obj":"http://purl.obolibrary.org/obo/GO_0045087"},{"id":"T48","span":{"begin":295,"end":304},"obj":"http://purl.obolibrary.org/obo/GO_0023052"},{"id":"T49","span":{"begin":405,"end":420},"obj":"http://purl.obolibrary.org/obo/GO_0045087"},{"id":"T50","span":{"begin":569,"end":586},"obj":"http://purl.obolibrary.org/obo/GO_0006952"},{"id":"T51","span":{"begin":726,"end":739},"obj":"http://purl.obolibrary.org/obo/GO_0045087"},{"id":"T52","span":{"begin":2919,"end":2932},"obj":"http://purl.obolibrary.org/obo/GO_0045087"},{"id":"T53","span":{"begin":3122,"end":3135},"obj":"http://purl.obolibrary.org/obo/GO_0045087"}],"text":"Molecular interactions and binding conformation of the designed MEPVC with TLR3 and TLR4 innate immune receptors were deciphered via a protein-peptide docking approach. Both TLR3 and TLR4 belong to toll-like receptor family of pattern recognition receptor and function to activate intracellular signaling NF-κB pathway and production of inflammatory cytokines responsible for the development of effective innate immunity [79,80]. These receptors recognize viral associated molecular patterns and induce the production of interferon leading to activation of strong host defense responses. Also, the specific adaptive immunity takes time to establish against antigens therefore it's important to evaluate MEPVC affinity for the innate immune receptors. In case of MRPVC-TLR3 complex, the patch dock predicted 10 best solutions sorted based on the docking geometric shape complementarity score (S-Table 3). A high score implies enhanced affinity of the interacting molecules and best docked conformations of the molecules with respect to each other. Solution 3 was visualized for docked conformations and intermolecular forces responsible for such high affinity of the molecules. The selection was based on the FireDock analysis (S-Table 4) which is an efficient package for refinement and reassigning procedure of docking scores to rigid body docking solutions. The global binding energy of solution 3 is better i.e. -6.39 kJ/mol compared to the rest of predicted solutions. The contribution to the total score form attractive van der Waals (VdW) energy is -12.12 kJ/mol, repulsive (VdW) energy (4.79 kJ/mol), hydrogen bond (HB) energy (-1.63 kJ/mol), and atomic contact energy (ACE) (5.95 kJ/mol). The MEPVC, within 3 Å, was noticed to posed right in the center of the TLR3 receptor (Figure 7 ) interacting via hydrogen and hydrophobic bonds with His156, Asp180, Lys201, Glu203, Ser206, Phe227, Asp229, Asp230, Ser254, Ser256, Asp257, Ser282, Tyr283, Asp284, Asp285, Glu301, Tyr302, Phe304, Glu306, Tyr307, Arg325, Glu358, His359, Lys382, Tyr383, P408, His410, Iso411, Gly431, His432, Glu434, Pro408, Asp457, Phe459, Gln483, and Glu533. Similarly, among 10 predicted MEPVC-TLR4 complexes (S-Table 5), solution 7 (S-Table 6) was affirmed as best with total global energy of -10.39 kJ/mol whereas the rest of complexes were noticed as highly unstable with score in positive. The attractive VdW, repulsive VdW, HB and ACE contribution to the global energy is -35.75 kJ/mol, 22.04 kJ/mol, -5.51 kJ/mol, and 12.61 kJ/mol, respectively. Visual analysis of the complex revealed binding of the MEPVC at the interface of chains B and D (Figure 8 ). The MEPVC is surrounded by chain B residues: Pro23, Glu24, Ser25, Asp44, Lys47, Asp50, Asp51, Arg67, Arg87, Glu89, Pro113, Gln115, Asp137, His159, Asp160, Ser184, and Lys186 and chain D residues: Lys20, Phe64, and Asp114.\nFig. 7 Binding conformation of MEPVC with respect to TLR3 innate immune receptor. The yellow labeled region pointing to the residues involved in both hydrophobic and hydrophilic interactions with MEPVC.\nFig. 8 Binding conformation of MEPVC with respect to TLR4 innate immune receptor. The yellow labeled region pointing to the residues involved in both hydrophobic and hydrophilic interactions with MEPVC."}

LitCovid-sentences

{"project":"LitCovid-sentences","denotations":[{"id":"T271","span":{"begin":0,"end":168},"obj":"Sentence"},{"id":"T272","span":{"begin":169,"end":429},"obj":"Sentence"},{"id":"T273","span":{"begin":430,"end":587},"obj":"Sentence"},{"id":"T274","span":{"begin":588,"end":750},"obj":"Sentence"},{"id":"T275","span":{"begin":751,"end":903},"obj":"Sentence"},{"id":"T276","span":{"begin":904,"end":1046},"obj":"Sentence"},{"id":"T277","span":{"begin":1047,"end":1176},"obj":"Sentence"},{"id":"T278","span":{"begin":1177,"end":1359},"obj":"Sentence"},{"id":"T279","span":{"begin":1360,"end":1472},"obj":"Sentence"},{"id":"T280","span":{"begin":1473,"end":1696},"obj":"Sentence"},{"id":"T281","span":{"begin":1697,"end":2135},"obj":"Sentence"},{"id":"T282","span":{"begin":2136,"end":2371},"obj":"Sentence"},{"id":"T283","span":{"begin":2372,"end":2529},"obj":"Sentence"},{"id":"T284","span":{"begin":2530,"end":2638},"obj":"Sentence"},{"id":"T285","span":{"begin":2639,"end":2683},"obj":"Sentence"},{"id":"T286","span":{"begin":2684,"end":2834},"obj":"Sentence"},{"id":"T287","span":{"begin":2835,"end":2860},"obj":"Sentence"},{"id":"T288","span":{"begin":2861,"end":2942},"obj":"Sentence"},{"id":"T289","span":{"begin":2943,"end":3063},"obj":"Sentence"},{"id":"T290","span":{"begin":3064,"end":3145},"obj":"Sentence"},{"id":"T291","span":{"begin":3146,"end":3266},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Molecular interactions and binding conformation of the designed MEPVC with TLR3 and TLR4 innate immune receptors were deciphered via a protein-peptide docking approach. Both TLR3 and TLR4 belong to toll-like receptor family of pattern recognition receptor and function to activate intracellular signaling NF-κB pathway and production of inflammatory cytokines responsible for the development of effective innate immunity [79,80]. These receptors recognize viral associated molecular patterns and induce the production of interferon leading to activation of strong host defense responses. Also, the specific adaptive immunity takes time to establish against antigens therefore it's important to evaluate MEPVC affinity for the innate immune receptors. In case of MRPVC-TLR3 complex, the patch dock predicted 10 best solutions sorted based on the docking geometric shape complementarity score (S-Table 3). A high score implies enhanced affinity of the interacting molecules and best docked conformations of the molecules with respect to each other. Solution 3 was visualized for docked conformations and intermolecular forces responsible for such high affinity of the molecules. The selection was based on the FireDock analysis (S-Table 4) which is an efficient package for refinement and reassigning procedure of docking scores to rigid body docking solutions. The global binding energy of solution 3 is better i.e. -6.39 kJ/mol compared to the rest of predicted solutions. The contribution to the total score form attractive van der Waals (VdW) energy is -12.12 kJ/mol, repulsive (VdW) energy (4.79 kJ/mol), hydrogen bond (HB) energy (-1.63 kJ/mol), and atomic contact energy (ACE) (5.95 kJ/mol). The MEPVC, within 3 Å, was noticed to posed right in the center of the TLR3 receptor (Figure 7 ) interacting via hydrogen and hydrophobic bonds with His156, Asp180, Lys201, Glu203, Ser206, Phe227, Asp229, Asp230, Ser254, Ser256, Asp257, Ser282, Tyr283, Asp284, Asp285, Glu301, Tyr302, Phe304, Glu306, Tyr307, Arg325, Glu358, His359, Lys382, Tyr383, P408, His410, Iso411, Gly431, His432, Glu434, Pro408, Asp457, Phe459, Gln483, and Glu533. Similarly, among 10 predicted MEPVC-TLR4 complexes (S-Table 5), solution 7 (S-Table 6) was affirmed as best with total global energy of -10.39 kJ/mol whereas the rest of complexes were noticed as highly unstable with score in positive. The attractive VdW, repulsive VdW, HB and ACE contribution to the global energy is -35.75 kJ/mol, 22.04 kJ/mol, -5.51 kJ/mol, and 12.61 kJ/mol, respectively. Visual analysis of the complex revealed binding of the MEPVC at the interface of chains B and D (Figure 8 ). The MEPVC is surrounded by chain B residues: Pro23, Glu24, Ser25, Asp44, Lys47, Asp50, Asp51, Arg67, Arg87, Glu89, Pro113, Gln115, Asp137, His159, Asp160, Ser184, and Lys186 and chain D residues: Lys20, Phe64, and Asp114.\nFig. 7 Binding conformation of MEPVC with respect to TLR3 innate immune receptor. The yellow labeled region pointing to the residues involved in both hydrophobic and hydrophilic interactions with MEPVC.\nFig. 8 Binding conformation of MEPVC with respect to TLR4 innate immune receptor. The yellow labeled region pointing to the residues involved in both hydrophobic and hydrophilic interactions with MEPVC."}

2_test

{"project":"2_test","denotations":[{"id":"32454128-25071777-29238342","span":{"begin":422,"end":424},"obj":"25071777"},{"id":"32454128-27162029-29238343","span":{"begin":425,"end":427},"obj":"27162029"}],"text":"Molecular interactions and binding conformation of the designed MEPVC with TLR3 and TLR4 innate immune receptors were deciphered via a protein-peptide docking approach. Both TLR3 and TLR4 belong to toll-like receptor family of pattern recognition receptor and function to activate intracellular signaling NF-κB pathway and production of inflammatory cytokines responsible for the development of effective innate immunity [79,80]. These receptors recognize viral associated molecular patterns and induce the production of interferon leading to activation of strong host defense responses. Also, the specific adaptive immunity takes time to establish against antigens therefore it's important to evaluate MEPVC affinity for the innate immune receptors. In case of MRPVC-TLR3 complex, the patch dock predicted 10 best solutions sorted based on the docking geometric shape complementarity score (S-Table 3). A high score implies enhanced affinity of the interacting molecules and best docked conformations of the molecules with respect to each other. Solution 3 was visualized for docked conformations and intermolecular forces responsible for such high affinity of the molecules. The selection was based on the FireDock analysis (S-Table 4) which is an efficient package for refinement and reassigning procedure of docking scores to rigid body docking solutions. The global binding energy of solution 3 is better i.e. -6.39 kJ/mol compared to the rest of predicted solutions. The contribution to the total score form attractive van der Waals (VdW) energy is -12.12 kJ/mol, repulsive (VdW) energy (4.79 kJ/mol), hydrogen bond (HB) energy (-1.63 kJ/mol), and atomic contact energy (ACE) (5.95 kJ/mol). The MEPVC, within 3 Å, was noticed to posed right in the center of the TLR3 receptor (Figure 7 ) interacting via hydrogen and hydrophobic bonds with His156, Asp180, Lys201, Glu203, Ser206, Phe227, Asp229, Asp230, Ser254, Ser256, Asp257, Ser282, Tyr283, Asp284, Asp285, Glu301, Tyr302, Phe304, Glu306, Tyr307, Arg325, Glu358, His359, Lys382, Tyr383, P408, His410, Iso411, Gly431, His432, Glu434, Pro408, Asp457, Phe459, Gln483, and Glu533. Similarly, among 10 predicted MEPVC-TLR4 complexes (S-Table 5), solution 7 (S-Table 6) was affirmed as best with total global energy of -10.39 kJ/mol whereas the rest of complexes were noticed as highly unstable with score in positive. The attractive VdW, repulsive VdW, HB and ACE contribution to the global energy is -35.75 kJ/mol, 22.04 kJ/mol, -5.51 kJ/mol, and 12.61 kJ/mol, respectively. Visual analysis of the complex revealed binding of the MEPVC at the interface of chains B and D (Figure 8 ). The MEPVC is surrounded by chain B residues: Pro23, Glu24, Ser25, Asp44, Lys47, Asp50, Asp51, Arg67, Arg87, Glu89, Pro113, Gln115, Asp137, His159, Asp160, Ser184, and Lys186 and chain D residues: Lys20, Phe64, and Asp114.\nFig. 7 Binding conformation of MEPVC with respect to TLR3 innate immune receptor. The yellow labeled region pointing to the residues involved in both hydrophobic and hydrophilic interactions with MEPVC.\nFig. 8 Binding conformation of MEPVC with respect to TLR4 innate immune receptor. The yellow labeled region pointing to the residues involved in both hydrophobic and hydrophilic interactions with MEPVC."}

MyTest

{"project":"MyTest","denotations":[{"id":"32454128-25071777-29238342","span":{"begin":422,"end":424},"obj":"25071777"},{"id":"32454128-27162029-29238343","span":{"begin":425,"end":427},"obj":"27162029"}],"namespaces":[{"prefix":"_base","uri":"https://www.uniprot.org/uniprot/testbase"},{"prefix":"UniProtKB","uri":"https://www.uniprot.org/uniprot/"},{"prefix":"uniprot","uri":"https://www.uniprot.org/uniprotkb/"}],"text":"Molecular interactions and binding conformation of the designed MEPVC with TLR3 and TLR4 innate immune receptors were deciphered via a protein-peptide docking approach. Both TLR3 and TLR4 belong to toll-like receptor family of pattern recognition receptor and function to activate intracellular signaling NF-κB pathway and production of inflammatory cytokines responsible for the development of effective innate immunity [79,80]. These receptors recognize viral associated molecular patterns and induce the production of interferon leading to activation of strong host defense responses. Also, the specific adaptive immunity takes time to establish against antigens therefore it's important to evaluate MEPVC affinity for the innate immune receptors. In case of MRPVC-TLR3 complex, the patch dock predicted 10 best solutions sorted based on the docking geometric shape complementarity score (S-Table 3). A high score implies enhanced affinity of the interacting molecules and best docked conformations of the molecules with respect to each other. Solution 3 was visualized for docked conformations and intermolecular forces responsible for such high affinity of the molecules. The selection was based on the FireDock analysis (S-Table 4) which is an efficient package for refinement and reassigning procedure of docking scores to rigid body docking solutions. The global binding energy of solution 3 is better i.e. -6.39 kJ/mol compared to the rest of predicted solutions. The contribution to the total score form attractive van der Waals (VdW) energy is -12.12 kJ/mol, repulsive (VdW) energy (4.79 kJ/mol), hydrogen bond (HB) energy (-1.63 kJ/mol), and atomic contact energy (ACE) (5.95 kJ/mol). The MEPVC, within 3 Å, was noticed to posed right in the center of the TLR3 receptor (Figure 7 ) interacting via hydrogen and hydrophobic bonds with His156, Asp180, Lys201, Glu203, Ser206, Phe227, Asp229, Asp230, Ser254, Ser256, Asp257, Ser282, Tyr283, Asp284, Asp285, Glu301, Tyr302, Phe304, Glu306, Tyr307, Arg325, Glu358, His359, Lys382, Tyr383, P408, His410, Iso411, Gly431, His432, Glu434, Pro408, Asp457, Phe459, Gln483, and Glu533. Similarly, among 10 predicted MEPVC-TLR4 complexes (S-Table 5), solution 7 (S-Table 6) was affirmed as best with total global energy of -10.39 kJ/mol whereas the rest of complexes were noticed as highly unstable with score in positive. The attractive VdW, repulsive VdW, HB and ACE contribution to the global energy is -35.75 kJ/mol, 22.04 kJ/mol, -5.51 kJ/mol, and 12.61 kJ/mol, respectively. Visual analysis of the complex revealed binding of the MEPVC at the interface of chains B and D (Figure 8 ). The MEPVC is surrounded by chain B residues: Pro23, Glu24, Ser25, Asp44, Lys47, Asp50, Asp51, Arg67, Arg87, Glu89, Pro113, Gln115, Asp137, His159, Asp160, Ser184, and Lys186 and chain D residues: Lys20, Phe64, and Asp114.\nFig. 7 Binding conformation of MEPVC with respect to TLR3 innate immune receptor. The yellow labeled region pointing to the residues involved in both hydrophobic and hydrophilic interactions with MEPVC.\nFig. 8 Binding conformation of MEPVC with respect to TLR4 innate immune receptor. The yellow labeled region pointing to the residues involved in both hydrophobic and hydrophilic interactions with MEPVC."}

PMC:7245302 / 35890-39156 JSONTXT

Annnotations TAB JSON ListView MergeView

PMC:7245302 / 35890-39156 JSON TXT