LitCovid-sentences  

PMC:7605337 / 51702-54287 JSONTXT 6 Projects

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Id Subject Object Predicate Lexical cue
T348 0-114 Sentence denotes Important mutations found in naturally occurring nCOV-2019 appear to influence to some extent the binding to ACE2.
T349 115-276 Sentence denotes Mutation T478I which is one of the most frequent mutations according to GISAID database, increases the binding affinity of nCOV-2019 to ACE2 by about 6 kcal/mol.
T350 277-458 Sentence denotes Mutation N439K has the highest occurrence among all strains of coronavirus in the GISAID database which demonstrated the highest electrostatic interaction among all studied systems.
T351 459-561 Sentence denotes This residue corresponds to R426 in SARS-COV which exerts a salt-bridge interaction with E329 on ACE2.
T352 562-688 Sentence denotes Mutation N439K recovers some of this ACE2 interaction; however, it exerts a binding affinity similar to that of wild-type RBD.
T353 689-831 Sentence denotes Contribution of important interface residues to binding affinity was compared for mutations T478I, N439K, and wild-type nCOV-2019 (Figure S7).
T354 832-1013 Sentence denotes The most striking differences between wild-type RBD and mutation T478I are residues Y449 and Q498 which have significantly higher contribution to binding than the wild type residue.
T355 1014-1100 Sentence denotes Most other residues at the interface have similar binding affinities to the nCOV-2019.
T356 1101-1287 Sentence denotes A higher H-bond persistence is also seen for these two residues Y449 and Q498 compared to the wild type RBD which is the reason for their higher contribution to the total binding energy.
T357 1288-1372 Sentence denotes Mutation N439K has a slightly lower binding affinity to ACE2 than the wild type RBD.
T358 1373-1640 Sentence denotes Per residue binding energy decomposition showed that K439 in this system has a favorable contribution of −1.80 ± 0.15 kcal/mol to the total binding energy which is balanced by a lower contribution of K417 which resulted in a binding affinity similar to wild-type RBD.
T359 1641-1781 Sentence denotes Mutant E484A, which is also one of the observed mutations based on GISAID database, demonstrates a high electrostatic interaction with ACE2.
T360 1782-1954 Sentence denotes E484 contributes to binding by 3.56 ± 0.15 kcal/mol whereas the corresponding residue in SARS-COV, P469 contributes to binding of SARS-COV to ACE2 by −0.27 ± 0.01 kcal/mol.
T361 1955-2042 Sentence denotes This residue is close to D30 on ACE2 and has electrostatic repulsion with this residue.
T362 2043-2386 Sentence denotes Most natural mutants including N439K, A475V, G476S, V483A, V483F, E484A, and S494P showed similar or slightly lower binding affinities to ACE2 compared to wild-type complex which agrees with experimental binding measurements.25 However, the experimental binding affinity for T478I also showed similar binding affinity to the wild-type complex.
T363 2387-2585 Sentence denotes This difference could be due to the use of MMPBSA approach for calculation of polar solvation and further studies are needed to study the effect of this mutation on viral infectivity of coronavirus.