3by1

<table><tr><td colspan='2'>[[3by1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Norwalk_calicivirus Norwalk calicivirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BY1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3BY1 FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ihm|1ihm]], [[3by2|3by2]], [[3by3|3by3]]</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3by1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3by1 OCA], [http://pdbe.org/3by1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3by1 RCSB], [http://www.ebi.ac.uk/pdbsum/3by1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3by1 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/CAPSD_NVN68 CAPSD_NVN68]] Capsid protein self assembles to form an icosahedral capsid with a T=3 symmetry, about 38 nm in diameter, and consisting of 180 capsid proteins. A smaller form of capsid with a diameter of 23 nm might be capsid proteins assembled as icosahedron with T=1 symmetry. The capsid encapsulate the genomic RNA and VP2 proteins. Attaches virion to target cells by binding histo-blood group antigens present on gastroduodenal epithelial cells.<ref>PMID:16840313</ref> Soluble capsid protein may play a role in viral immunoevasion.<ref>PMID:16840313</ref>

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== Publication Abstract from PubMed ==

Noroviruses are positive-sense, single-stranded RNA viruses that cause acute gastroenteritis. They recognize human histo-blood group antigens as receptors in a strain-specific manner. The structures presented here were analyzed in order to elucidate the structural basis for differences in ligand recognition of noroviruses from different genogroups, the prototypic Norwalk virus (NV; GI-1) and VA387 (GII-4), which recognize the same A antigen but differ in that NV is unable to bind to the B antigen. Two forms of the receptor-binding domain of the norovirus coat protein, the P domain and the P polypeptide, that were previously shown to differ in receptor binding and P-particle formation properties were studied. Comparison of the structures of the NV P domain with and without A trisaccharide and the NV P polypeptide revealed no major ligand-induced changes. The 2.3-A cocrystal structure reveals that the A trisaccharide binds to the NV P domain through interactions with the residues Ser377, Asp327, His329, and Ser380 in a mode distinct from that previously reported for the VA387 P-domain-A-trisaccharide complex. Mutational analyses confirm the importance of these residues in NV P-particle binding to native A antigen. The alpha-GalNAc residue unique to the A trisaccharide is buried deeply in the NV binding pocket, unlike in the structures of A and B trisaccharides bound to VA387 P domain, where the alpha-fucose residue forms the most protein contacts. The A-trisaccharide binding mode seen in the NV P domain complex cannot be sterically accommodated in the VA387 P domain.

Structural basis for the receptor binding specificity of Norwalk virus.,Bu W, Mamedova A, Tan M, Xia M, Jiang X, Hegde RS J Virol. 2008 Jun;82(11):5340-7. Epub 2008 Apr 2. PMID:18385236<ref>PMID:18385236</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 3by1" style="background-color:#fffaf0;"></div>

[[Category: Norwalk calicivirus]]

[[Category: Bu, W]]

[[Category: Hegde, R]]

[[Category: Viral protein]]