3by2: Difference between revisions
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==Norwalk P polypeptide (228-523)== | ==Norwalk P polypeptide (228-523)== | ||
<StructureSection load='3by2' size='340' side='right' caption='[[3by2]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='3by2' size='340' side='right'caption='[[3by2]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3by2]] 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=3BY2 OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[3by2]] 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=3BY2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3BY2 FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ihm|1ihm]], [[3by1|3by1]], [[3by3|3by3]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ihm|1ihm]], [[3by1|3by1]], [[3by3|3by3]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3by2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3by2 OCA], [http://pdbe.org/3by2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3by2 RCSB], [http://www.ebi.ac.uk/pdbsum/3by2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3by2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| Line 30: | Line 30: | ||
==See Also== | ==See Also== | ||
*[[Virus coat | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Norwalk calicivirus]] | [[Category: Norwalk calicivirus]] | ||
[[Category: Bu, W]] | [[Category: Bu, W]] | ||
Revision as of 13:22, 12 August 2020
Norwalk P polypeptide (228-523)Norwalk P polypeptide (228-523)
Structural highlights
Function[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.[1] Soluble capsid protein may play a role in viral immunoevasion.[2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedNoroviruses 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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