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==CRYSTAL STRUCTURE ANALYSIS OF NORWALK VIRUS CAPSID==
==CRYSTAL STRUCTURE ANALYSIS OF NORWALK VIRUS CAPSID==
<StructureSection load='1ihm' size='340' side='right' caption='[[1ihm]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
<StructureSection load='1ihm' size='340' side='right'caption='[[1ihm]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ihm]] is a 3 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=1IHM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IHM FirstGlance]. <br>
<table><tr><td colspan='2'>[[1ihm]] is a 3 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=1IHM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IHM FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ihm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ihm OCA], [http://pdbe.org/1ihm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ihm RCSB], [http://www.ebi.ac.uk/pdbsum/1ihm PDBsum]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.4&#8491;</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=1ihm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ihm OCA], [https://pdbe.org/1ihm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ihm RCSB], [https://www.ebi.ac.uk/pdbsum/1ihm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ihm ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[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>
[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>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ih/1ihm_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ih/1ihm_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
</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].
</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=1ihm ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Norwalk virus, a noncultivatable human calicivirus, is the major cause of epidemic gastroenteritis in humans. The first x-ray structure of a calicivirus capsid, which consists of 180 copies of a single protein, has been determined by phase extension from a low-resolution electron microscopy structure. The capsid protein has a protruding (P) domain connected by a flexible hinge to a shell (S) domain that has a classical eight-stranded beta-sandwich motif. The structure of the P domain is unlike that of any other viral protein with a subdomain exhibiting a fold similar to that of the second domain in the eukaryotic translation elongation factor-Tu. This subdomain, located at the exterior of the capsid, has the largest sequence variation among Norwalk-like human caliciviruses and is likely to contain the determinants of strain specificity and cell binding.
X-ray crystallographic structure of the Norwalk virus capsid.,Prasad BV, Hardy ME, Dokland T, Bella J, Rossmann MG, Estes MK Science. 1999 Oct 8;286(5438):287-90. PMID:10514371<ref>PMID:10514371</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ihm" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Virus coat protein|Virus coat protein]]
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Norwalk calicivirus]]
[[Category: Large Structures]]
[[Category: Bella, J]]
[[Category: Norwalk virus]]
[[Category: Dokland, T]]
[[Category: Bella J]]
[[Category: Estes, M K]]
[[Category: Dokland T]]
[[Category: Hardy, M E]]
[[Category: Estes MK]]
[[Category: Prasad, B V]]
[[Category: Hardy ME]]
[[Category: Rossmann, M G]]
[[Category: Prasad BV]]
[[Category: Beta-barrel]]
[[Category: Rossmann MG]]
[[Category: Ef-tu-like domain caliciviridae]]
[[Category: Icosahedral virus]]
[[Category: T=3 icosahedral capsid]]
[[Category: Virus]]

Latest revision as of 09:02, 3 April 2024

CRYSTAL STRUCTURE ANALYSIS OF NORWALK VIRUS CAPSIDCRYSTAL STRUCTURE ANALYSIS OF NORWALK VIRUS CAPSID

Structural highlights

1ihm is a 3 chain structure with sequence from Norwalk virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.4Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

See Also

References

  1. ↑ Tan M, Meller J, Jiang X. C-terminal arginine cluster is essential for receptor binding of norovirus capsid protein. J Virol. 2006 Aug;80(15):7322-31. PMID:16840313 doi:http://dx.doi.org/80/15/7322
  2. ↑ Tan M, Meller J, Jiang X. C-terminal arginine cluster is essential for receptor binding of norovirus capsid protein. J Virol. 2006 Aug;80(15):7322-31. PMID:16840313 doi:http://dx.doi.org/80/15/7322

1ihm, resolution 3.40Å

Drag the structure with the mouse to rotate

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