3asp: Difference between revisions
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==Crystal structure of P domain from Norovirus Funabashi258 stain in the complex with A-antigen== | ==Crystal structure of P domain from Norovirus Funabashi258 stain in the complex with A-antigen== | ||
<StructureSection load='3asp' size='340' side='right' caption='[[3asp]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='3asp' size='340' side='right' caption='[[3asp]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3asq|3asq]], [[3asr|3asr]], [[3ass|3ass]], [[3ast|3ast]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3asq|3asq]], [[3asr|3asr]], [[3ass|3ass]], [[3ast|3ast]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">capsid, ORF2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=95340 Norwalk like virus])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">capsid, ORF2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=95340 Norwalk like virus])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3asp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3asp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3asp RCSB], [http://www.ebi.ac.uk/pdbsum/3asp PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3asp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3asp OCA], [http://pdbe.org/3asp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3asp RCSB], [http://www.ebi.ac.uk/pdbsum/3asp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3asp ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3asp" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 18:19, 5 August 2016
Crystal structure of P domain from Norovirus Funabashi258 stain in the complex with A-antigenCrystal structure of P domain from Norovirus Funabashi258 stain in the complex with A-antigen
Structural highlights
Publication Abstract from PubMedNoroviruses (NoVs) bind to histo-blood group antigens, namely, ABH antigens and Lewis antigens. We previously showed the NoVs GI/2, GI/3, GI/4, and GI/8 were able to strongly bind to Lewis a (Le(a)) antigen, which is expressed by individuals who are nonsecretors. In this study, to investigate how Lewis antigens interact with GI NoV virion protein 1 (VP1), we determined the crystal structures of the P domain of the VP1 protein from the Funabashi 258 (FUV258) strain (GI/2) in complexes with Le(a), Le(b), H type 1, or A type 1 antigens. The structures were compared with those of the NV/68 strain (GI/1), which does not bind to the Le(a) antigen. The four loop structures, loop P, loop S, loop A, and loop B, continuously deviated by more than 2 A in length between the Calpha atoms of the corresponding residues of the FUV258 and NV/68 P domains. The most pronounced differences between the two VP1 proteins were observed in the structures of loop P. In the FUV258 P domain, loop P protruded toward the next protomer, forming a Le(a) antigen-binding site. The Gln389 residue make a significant contribution to the binding of the Le(a) antigen through the stabilization of loop P as well as through direct interactions with the alpha4-fucosyl residue (alpha4Fuc) of the Le(a) antigen. Mutation of the Gln389 residue dramatically affected the degree of binding of the Lewis antigens. Collectively, these results suggest that loop P and the amino acid residue at position 389 affect Lewis antigen binding. Structural basis for the recognition of Lewis antigens by genogroup I norovirus.,Kubota T, Kumagai A, Ito H, Furukawa S, Someya Y, Takeda N, Ishii K, Wakita T, Narimatsu H, Shirato H J Virol. 2012 Oct;86(20):11138-50. Epub 2012 Aug 1. PMID:22855491[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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