1k3v
From Proteopedia
(Difference between revisions)
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<StructureSection load='1k3v' size='340' side='right'caption='[[1k3v]], [[Resolution|resolution]] 3.50Å' scene=''> | <StructureSection load='1k3v' size='340' side='right'caption='[[1k3v]], [[Resolution|resolution]] 3.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1k3v]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1k3v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Porcine_parvovirus Porcine parvovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K3V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K3V FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5Å</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=1k3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k3v OCA], [https://pdbe.org/1k3v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k3v RCSB], [https://www.ebi.ac.uk/pdbsum/1k3v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k3v ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/CAPSD_PAVPN CAPSD_PAVPN] Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 22 nm in diameter, and consisting of 60 copies of two size variants of the capsid proteins, VP1 and VP2, which differ by the presence of an N-terminal extension in the minor protein VP1. The capsid encapsulates the genomic ssDNA. Capsid proteins are responsible for the attachment to host cell receptors. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. Binding to the host receptors also induces capsid rearrangements leading to surface exposure of VP1 N-terminus, specifically its phospholipase A2-like region and putative nuclear localization signal(s). VP1 N-terminus might serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell and might contribute to virus transport to the nucleus (By similarity). |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[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=1k3v 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=1k3v ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The structure of baculovirus-expressed porcine parvovirus (PPV) capsids was solved using X-ray crystallography and was found to be similar to the related canine parvovirus (CPV) and minute virus of mice (MVM). The PPV capsid protein has 57 % and 49 % amino acid sequence identity with CPV and MVM, respectively, but the degree of conservation of surface-exposed residues is lower than average. Consequently, most of the structural differences are on the surface and are the probable cause of the known variability in antigenicity and host range. The NADL-2 and Kresse strains of PPV have distinct tissue tropisms and pathogenicity, which are mediated by one or more of the amino acid residues 381, 386, and 436. These residues are on or near the surface of the virus capsid, where they are likely to be associated with virus-cell interactions. | ||
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| - | The structure of porcine parvovirus: comparison with related viruses.,Simpson AA, Hebert B, Sullivan GM, Parrish CR, Zadori Z, Tijssen P, Rossmann MG J Mol Biol. 2002 Feb 1;315(5):1189-98. PMID:11827486<ref>PMID:11827486</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1k3v" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Porcine parvovirus]] |
| - | [[Category: Hebert | + | [[Category: Hebert B]] |
| - | [[Category: Parrish | + | [[Category: Parrish CR]] |
| - | [[Category: Rossmann | + | [[Category: Rossmann MG]] |
| - | [[Category: Simpson | + | [[Category: Simpson AA]] |
| - | [[Category: Sullivan | + | [[Category: Sullivan GM]] |
| - | [[Category: Tijssen | + | [[Category: Tijssen P]] |
| - | [[Category: Zadori | + | [[Category: Zadori Z]] |
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Current revision
Porcine Parvovirus Capsid
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