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2obr

From Proteopedia

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[[Image:2obr.png|left|200px]]
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==Crystal Structures of P Domain of Norovirus VA387==
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<StructureSection load='2obr' size='340' side='right' caption='[[2obr]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2obr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Norovirus Norovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OBR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2OBR FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2obr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2obr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2obr RCSB], [http://www.ebi.ac.uk/pdbsum/2obr PDBsum]</span></td></tr>
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<table>
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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/ob/2obr_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/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Noroviruses are one of the major causes of nonbacterial gastroenteritis epidemics in humans. Recent studies on norovirus receptors show that different noroviruses recognize different human histo-blood group antigens (HBGAs), and eight receptor binding patterns of noroviruses have been identified. The P domain of the norovirus capsids is directly involved in this recognition. To determine the precise locations and receptor binding modes of HBGA carbohydrates on the viral capsids, a recombinant P protein of a GII-4 strain norovirus, VA387, was cocrystallized with synthetic type A or B trisaccharides. Based on complex crystal structures observed at a 2.0-A resolution, we demonstrated that the receptor binding site lies at the outermost end of the P domain and forms an extensive hydrogen-bonding network with the saccharide ligand. The A and B trisaccharides display similar binding modes, and the common fucose ring plays a key role in this interaction. The extensive interface between the two protomers in a P dimer also plays a crucial role in the formation of the receptor binding interface.
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{{STRUCTURE_2obr| PDB=2obr | SCENE= }}
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Structural basis for the recognition of blood group trisaccharides by norovirus.,Cao S, Lou Z, Tan M, Chen Y, Liu Y, Zhang Z, Zhang XC, Jiang X, Li X, Rao Z J Virol. 2007 Jun;81(11):5949-57. Epub 2007 Mar 28. PMID:17392366<ref>PMID:17392366</ref>
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===Crystal Structures of P Domain of Norovirus VA387===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_17392366}}
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==About this Structure==
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[[2obr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Norovirus Norovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OBR OCA].
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==See Also==
==See Also==
*[[Virus coat protein|Virus coat protein]]
*[[Virus coat protein|Virus coat protein]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:017392366</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Norovirus]]
[[Category: Norovirus]]
[[Category: Cao, S.]]
[[Category: Cao, S.]]

Revision as of 03:12, 29 September 2014

Crystal Structures of P Domain of Norovirus VA387

2obr, resolution 2.20Å

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