PMC:7094172 / 8581-10117 JSONTXT

{"project":"LitCovid-PMC-OGER-BB","denotations":[{"id":"T669","span":{"begin":26,"end":34},"obj":"SP_9"},{"id":"T668","span":{"begin":71,"end":79},"obj":"SP_9"},{"id":"T667","span":{"begin":210,"end":222},"obj":"GO:0046983"},{"id":"T666","span":{"begin":290,"end":298},"obj":"SP_9"},{"id":"T665","span":{"begin":307,"end":319},"obj":"GO:0051260"},{"id":"T664","span":{"begin":342,"end":348},"obj":"SO:0000440"},{"id":"T663","span":{"begin":875,"end":881},"obj":"SO:0000440"},{"id":"T662","span":{"begin":1156,"end":1162},"obj":"SO:0000440"},{"id":"T661","span":{"begin":1430,"end":1448},"obj":"SO:0000366"},{"id":"T660","span":{"begin":1490,"end":1502},"obj":"GO:0046983"}],"text":"Structure and sequence of MERS-CoV N-NTD. (A) Overall structure of the MERS-CoV N-NTD dimer containing monomers 1 and 2 is depicted as a cartoon and colored yellow and green, respectively. Residues involved in dimerization are shown as sticks and highlighted in (B). (B) Interactions among MERS-CoV N-NTDs. Dimerization is mediated mainly by vector-fusion residues interacting with the conserved hydrophobic regions on the core structure (first area) along with the residues surrounding it (second area). Interacting residues on monomers 1 and 2 are labeled in black and blue, respectively. Vector-fusion and conserved hydrophobic regions are colored cyan and red, respectively. The color of all other interacting residues is the same as that for each monomer in (A). Polar contacts are indicated with red dashed lines. (C) Upper panel: close-up of the interacting region of vector-fusion residues. The surface was colored according to the hydrophobicity level at the protein surface. Vector-fusion residues (black) are shown as sticks to emphasize the hydrophobic pocket. Lower panel: 2D diagrams of the interaction between the hydrophobic pocket and the vector-fusion residues. The latter are labeled in black. The hydrophobic contacts are indicated with black dashed lines. (D) Sequence alignment of various CoV N proteins in the N-terminal region. Red letters indicate strictly conserved residues. Cyan indicates conservative substitution sites. Hydrophobic regions involved in unusual dimerization are indicated by black triangles."}

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T42","span":{"begin":968,"end":975},"obj":"Body_part"},{"id":"T43","span":{"begin":1317,"end":1325},"obj":"Body_part"}],"attributes":[{"id":"A42","pred":"fma_id","subj":"T42","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A43","pred":"fma_id","subj":"T43","obj":"http://purl.org/sig/ont/fma/fma67257"}],"text":"Structure and sequence of MERS-CoV N-NTD. (A) Overall structure of the MERS-CoV N-NTD dimer containing monomers 1 and 2 is depicted as a cartoon and colored yellow and green, respectively. Residues involved in dimerization are shown as sticks and highlighted in (B). (B) Interactions among MERS-CoV N-NTDs. Dimerization is mediated mainly by vector-fusion residues interacting with the conserved hydrophobic regions on the core structure (first area) along with the residues surrounding it (second area). Interacting residues on monomers 1 and 2 are labeled in black and blue, respectively. Vector-fusion and conserved hydrophobic regions are colored cyan and red, respectively. The color of all other interacting residues is the same as that for each monomer in (A). Polar contacts are indicated with red dashed lines. (C) Upper panel: close-up of the interacting region of vector-fusion residues. The surface was colored according to the hydrophobicity level at the protein surface. Vector-fusion residues (black) are shown as sticks to emphasize the hydrophobic pocket. Lower panel: 2D diagrams of the interaction between the hydrophobic pocket and the vector-fusion residues. The latter are labeled in black. The hydrophobic contacts are indicated with black dashed lines. (D) Sequence alignment of various CoV N proteins in the N-terminal region. Red letters indicate strictly conserved residues. Cyan indicates conservative substitution sites. Hydrophobic regions involved in unusual dimerization are indicated by black triangles."}

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T37","span":{"begin":37,"end":40},"obj":"Disease"},{"id":"T39","span":{"begin":82,"end":85},"obj":"Disease"}],"attributes":[{"id":"A37","pred":"mondo_id","subj":"T37","obj":"http://purl.obolibrary.org/obo/MONDO_0008449"},{"id":"A38","pred":"mondo_id","subj":"T37","obj":"http://purl.obolibrary.org/obo/MONDO_0018075"},{"id":"A39","pred":"mondo_id","subj":"T39","obj":"http://purl.obolibrary.org/obo/MONDO_0008449"},{"id":"A40","pred":"mondo_id","subj":"T39","obj":"http://purl.obolibrary.org/obo/MONDO_0018075"}],"text":"Structure and sequence of MERS-CoV N-NTD. (A) Overall structure of the MERS-CoV N-NTD dimer containing monomers 1 and 2 is depicted as a cartoon and colored yellow and green, respectively. Residues involved in dimerization are shown as sticks and highlighted in (B). (B) Interactions among MERS-CoV N-NTDs. Dimerization is mediated mainly by vector-fusion residues interacting with the conserved hydrophobic regions on the core structure (first area) along with the residues surrounding it (second area). Interacting residues on monomers 1 and 2 are labeled in black and blue, respectively. Vector-fusion and conserved hydrophobic regions are colored cyan and red, respectively. The color of all other interacting residues is the same as that for each monomer in (A). Polar contacts are indicated with red dashed lines. (C) Upper panel: close-up of the interacting region of vector-fusion residues. The surface was colored according to the hydrophobicity level at the protein surface. Vector-fusion residues (black) are shown as sticks to emphasize the hydrophobic pocket. Lower panel: 2D diagrams of the interaction between the hydrophobic pocket and the vector-fusion residues. The latter are labeled in black. The hydrophobic contacts are indicated with black dashed lines. (D) Sequence alignment of various CoV N proteins in the N-terminal region. Red letters indicate strictly conserved residues. Cyan indicates conservative substitution sites. Hydrophobic regions involved in unusual dimerization are indicated by black triangles."}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T60","span":{"begin":43,"end":44},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T61","span":{"begin":135,"end":136},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T62","span":{"begin":263,"end":269},"obj":"http://purl.obolibrary.org/obo/CLO_0001869"},{"id":"T63","span":{"begin":550,"end":557},"obj":"http://purl.obolibrary.org/obo/CLO_0007225"},{"id":"T64","span":{"begin":764,"end":765},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T65","span":{"begin":1195,"end":1202},"obj":"http://purl.obolibrary.org/obo/CLO_0007225"}],"text":"Structure and sequence of MERS-CoV N-NTD. (A) Overall structure of the MERS-CoV N-NTD dimer containing monomers 1 and 2 is depicted as a cartoon and colored yellow and green, respectively. Residues involved in dimerization are shown as sticks and highlighted in (B). (B) Interactions among MERS-CoV N-NTDs. Dimerization is mediated mainly by vector-fusion residues interacting with the conserved hydrophobic regions on the core structure (first area) along with the residues surrounding it (second area). Interacting residues on monomers 1 and 2 are labeled in black and blue, respectively. Vector-fusion and conserved hydrophobic regions are colored cyan and red, respectively. The color of all other interacting residues is the same as that for each monomer in (A). Polar contacts are indicated with red dashed lines. (C) Upper panel: close-up of the interacting region of vector-fusion residues. The surface was colored according to the hydrophobicity level at the protein surface. Vector-fusion residues (black) are shown as sticks to emphasize the hydrophobic pocket. Lower panel: 2D diagrams of the interaction between the hydrophobic pocket and the vector-fusion residues. The latter are labeled in black. The hydrophobic contacts are indicated with black dashed lines. (D) Sequence alignment of various CoV N proteins in the N-terminal region. Red letters indicate strictly conserved residues. Cyan indicates conservative substitution sites. Hydrophobic regions involved in unusual dimerization are indicated by black triangles."}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T74","span":{"begin":968,"end":975},"obj":"Chemical"},{"id":"T75","span":{"begin":1317,"end":1325},"obj":"Chemical"}],"attributes":[{"id":"A74","pred":"chebi_id","subj":"T74","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A75","pred":"chebi_id","subj":"T75","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"}],"text":"Structure and sequence of MERS-CoV N-NTD. (A) Overall structure of the MERS-CoV N-NTD dimer containing monomers 1 and 2 is depicted as a cartoon and colored yellow and green, respectively. Residues involved in dimerization are shown as sticks and highlighted in (B). (B) Interactions among MERS-CoV N-NTDs. Dimerization is mediated mainly by vector-fusion residues interacting with the conserved hydrophobic regions on the core structure (first area) along with the residues surrounding it (second area). Interacting residues on monomers 1 and 2 are labeled in black and blue, respectively. Vector-fusion and conserved hydrophobic regions are colored cyan and red, respectively. The color of all other interacting residues is the same as that for each monomer in (A). Polar contacts are indicated with red dashed lines. (C) Upper panel: close-up of the interacting region of vector-fusion residues. The surface was colored according to the hydrophobicity level at the protein surface. Vector-fusion residues (black) are shown as sticks to emphasize the hydrophobic pocket. Lower panel: 2D diagrams of the interaction between the hydrophobic pocket and the vector-fusion residues. The latter are labeled in black. The hydrophobic contacts are indicated with black dashed lines. (D) Sequence alignment of various CoV N proteins in the N-terminal region. Red letters indicate strictly conserved residues. Cyan indicates conservative substitution sites. Hydrophobic regions involved in unusual dimerization are indicated by black triangles."}

{"project":"LitCovid-sentences","denotations":[{"id":"T60","span":{"begin":189,"end":306},"obj":"Sentence"},{"id":"T61","span":{"begin":307,"end":504},"obj":"Sentence"},{"id":"T62","span":{"begin":505,"end":590},"obj":"Sentence"},{"id":"T63","span":{"begin":591,"end":678},"obj":"Sentence"},{"id":"T64","span":{"begin":679,"end":767},"obj":"Sentence"},{"id":"T65","span":{"begin":768,"end":898},"obj":"Sentence"},{"id":"T66","span":{"begin":899,"end":984},"obj":"Sentence"},{"id":"T67","span":{"begin":985,"end":1072},"obj":"Sentence"},{"id":"T68","span":{"begin":1073,"end":1085},"obj":"Sentence"},{"id":"T69","span":{"begin":1086,"end":1179},"obj":"Sentence"},{"id":"T70","span":{"begin":1180,"end":1212},"obj":"Sentence"},{"id":"T71","span":{"begin":1213,"end":1351},"obj":"Sentence"},{"id":"T72","span":{"begin":1352,"end":1401},"obj":"Sentence"},{"id":"T73","span":{"begin":1402,"end":1449},"obj":"Sentence"},{"id":"T74","span":{"begin":1450,"end":1536},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Structure and sequence of MERS-CoV N-NTD. (A) Overall structure of the MERS-CoV N-NTD dimer containing monomers 1 and 2 is depicted as a cartoon and colored yellow and green, respectively. Residues involved in dimerization are shown as sticks and highlighted in (B). (B) Interactions among MERS-CoV N-NTDs. Dimerization is mediated mainly by vector-fusion residues interacting with the conserved hydrophobic regions on the core structure (first area) along with the residues surrounding it (second area). Interacting residues on monomers 1 and 2 are labeled in black and blue, respectively. Vector-fusion and conserved hydrophobic regions are colored cyan and red, respectively. The color of all other interacting residues is the same as that for each monomer in (A). Polar contacts are indicated with red dashed lines. (C) Upper panel: close-up of the interacting region of vector-fusion residues. The surface was colored according to the hydrophobicity level at the protein surface. Vector-fusion residues (black) are shown as sticks to emphasize the hydrophobic pocket. Lower panel: 2D diagrams of the interaction between the hydrophobic pocket and the vector-fusion residues. The latter are labeled in black. The hydrophobic contacts are indicated with black dashed lines. (D) Sequence alignment of various CoV N proteins in the N-terminal region. Red letters indicate strictly conserved residues. Cyan indicates conservative substitution sites. Hydrophobic regions involved in unusual dimerization are indicated by black triangles."}

{"project":"LitCovid-PubTator","denotations":[{"id":"131","span":{"begin":103,"end":119},"obj":"Gene"},{"id":"132","span":{"begin":529,"end":545},"obj":"Gene"},{"id":"133","span":{"begin":26,"end":34},"obj":"Species"},{"id":"134","span":{"begin":71,"end":79},"obj":"Species"},{"id":"135","span":{"begin":1311,"end":1314},"obj":"Species"},{"id":"136","span":{"begin":80,"end":85},"obj":"Chemical"},{"id":"137","span":{"begin":295,"end":305},"obj":"Disease"}],"attributes":[{"id":"A133","pred":"tao:has_database_id","subj":"133","obj":"Tax:1335626"},{"id":"A134","pred":"tao:has_database_id","subj":"134","obj":"Tax:1335626"},{"id":"A135","pred":"tao:has_database_id","subj":"135","obj":"Tax:11118"},{"id":"A137","pred":"tao:has_database_id","subj":"137","obj":"MESH:C000657245"}],"namespaces":[{"prefix":"Tax","uri":"https://www.ncbi.nlm.nih.gov/taxonomy/"},{"prefix":"MESH","uri":"https://id.nlm.nih.gov/mesh/"},{"prefix":"Gene","uri":"https://www.ncbi.nlm.nih.gov/gene/"},{"prefix":"CVCL","uri":"https://web.expasy.org/cellosaurus/CVCL_"}],"text":"Structure and sequence of MERS-CoV N-NTD. (A) Overall structure of the MERS-CoV N-NTD dimer containing monomers 1 and 2 is depicted as a cartoon and colored yellow and green, respectively. Residues involved in dimerization are shown as sticks and highlighted in (B). (B) Interactions among MERS-CoV N-NTDs. Dimerization is mediated mainly by vector-fusion residues interacting with the conserved hydrophobic regions on the core structure (first area) along with the residues surrounding it (second area). Interacting residues on monomers 1 and 2 are labeled in black and blue, respectively. Vector-fusion and conserved hydrophobic regions are colored cyan and red, respectively. The color of all other interacting residues is the same as that for each monomer in (A). Polar contacts are indicated with red dashed lines. (C) Upper panel: close-up of the interacting region of vector-fusion residues. The surface was colored according to the hydrophobicity level at the protein surface. Vector-fusion residues (black) are shown as sticks to emphasize the hydrophobic pocket. Lower panel: 2D diagrams of the interaction between the hydrophobic pocket and the vector-fusion residues. The latter are labeled in black. The hydrophobic contacts are indicated with black dashed lines. (D) Sequence alignment of various CoV N proteins in the N-terminal region. Red letters indicate strictly conserved residues. Cyan indicates conservative substitution sites. Hydrophobic regions involved in unusual dimerization are indicated by black triangles."}