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3by1

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(New page: 200px <!-- The line below this paragraph, containing "STRUCTURE_3by1", creates the "Structure Box" on the page. You may change the PDB parameter (which sets the PD...)
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[[Image:3by1.jpg|left|200px]]
 
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==Unliganded Norvalk Virus P domain==
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The line below this paragraph, containing "STRUCTURE_3by1", creates the "Structure Box" on the page.
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<StructureSection load='3by1' size='340' side='right'caption='[[3by1]], [[Resolution|resolution]] 2.69&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3by1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Norwalk_virus Norwalk virus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=3BY1 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.69&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3by1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3by1 OCA], [https://pdbe.org/3by1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3by1 RCSB], [https://www.ebi.ac.uk/pdbsum/3by1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3by1 ProSAT]</span></td></tr>
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{{STRUCTURE_3by1| PDB=3by1 | SCENE= }}
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</table>
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== Function ==
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[https://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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/by/3by1_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3by1 ConSurf].
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<div style="clear:both"></div>
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'''Unliganded Norvalk Virus P domain'''
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==See Also==
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*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
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== References ==
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==Overview==
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<references/>
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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 sought 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 the inability of NV 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 reveal no major ligand-induced changes. The 2.3 A co-crystal structure reveals that the A-trisaccharide binds to the NV P domain through interactions with 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.
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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3BY1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Norwalk_virus Norwalk virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BY1 OCA].
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==Reference==
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Structural basis for the receptor binding specificity of the Norwalk virus., Bu W, Mamedova A, Tan M, Xia M, Jiang X, Hegde RS, J Virol. 2008 Apr 2;. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18385236 18385236]
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[[Category: Norwalk virus]]
[[Category: Norwalk virus]]
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[[Category: Single protein]]
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[[Category: Bu W]]
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[[Category: Bu, W.]]
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[[Category: Hegde R]]
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[[Category: Hegde, R.]]
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[[Category: Norwalk virus p domain]]
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[[Category: Viral protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 24 09:49:59 2008''
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Current revision

Unliganded Norvalk Virus P domain

PDB ID 3by1

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