3asr: Difference between revisions
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<StructureSection load='3asr' size='340' side='right'caption='[[3asr]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='3asr' size='340' side='right'caption='[[3asr]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3asr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3asr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Norwalk-like_virus Norwalk-like virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ASR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ASR FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NPO:P-NITROPHENOL'>NPO</scene>, <scene name='pdbligand=PRD_900129:Lewis+A+antigen,+beta+anomer'>PRD_900129</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3asr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3asr OCA], [https://pdbe.org/3asr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3asr RCSB], [https://www.ebi.ac.uk/pdbsum/3asr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3asr ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3asr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3asr OCA], [https://pdbe.org/3asr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3asr RCSB], [https://www.ebi.ac.uk/pdbsum/3asr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3asr ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8JW44_9CALI Q8JW44_9CALI] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Norwalk like virus]] | [[Category: Norwalk-like virus]] | ||
[[Category: Furukawa | [[Category: Furukawa S]] | ||
[[Category: Ishii | [[Category: Ishii K]] | ||
[[Category: Itoh | [[Category: Itoh H]] | ||
[[Category: Kubota | [[Category: Kubota T]] | ||
[[Category: Kumagai | [[Category: Kumagai A]] | ||
[[Category: Narimatsu | [[Category: Narimatsu H]] | ||
[[Category: Shirato | [[Category: Shirato H]] | ||
[[Category: Someya | [[Category: Someya Y]] | ||
[[Category: Takeda | [[Category: Takeda N]] | ||
[[Category: Wakita | [[Category: Wakita T]] | ||
Latest revision as of 17:33, 1 November 2023
Crystal structure of P domain from Norovirus Funabashi258 stain in the complex with Lewis-aCrystal structure of P domain from Norovirus Funabashi258 stain in the complex with Lewis-a
Structural highlights
FunctionPublication 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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