1ihm: Difference between revisions

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 <StructureSection load='1ihm' size='340' side='right'caption='[[1ihm]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ihm]] is a 3 chain structure with sequence from [https://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 [https://proteopedia.org/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'>[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>
+</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>
 == Function ==
-[[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>
+[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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
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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=1ihm ConSurf].
 <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==
@@ Line 35: / Line 27: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Norwalk calicivirus]]
+[[Category: Norwalk virus]]
-[[Category: Bella, J]]
+[[Category: Bella J]]
-[[Category: Dokland, T]]
+[[Category: Dokland T]]
-[[Category: Estes, M K]]
+[[Category: Estes MK]]
-[[Category: Hardy, M E]]
+[[Category: Hardy ME]]
-[[Category: Prasad, B V]]
+[[Category: Prasad BV]]
-[[Category: Rossmann, M G]]
+[[Category: Rossmann MG]]
-[[Category: Beta-barrel]]
-[[Category: Ef-tu-like domain caliciviridae]]
-[[Category: Icosahedral virus]]
-[[Category: T=3 icosahedral capsid]]
-[[Category: Virus]]