1s58
From Proteopedia
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==The structure of B19 parvovirus capsid== | ==The structure of B19 parvovirus capsid== | ||
| - | <StructureSection load='1s58' size='340' side='right' caption='[[1s58]], [[Resolution|resolution]] 3.50Å' scene=''> | + | <StructureSection load='1s58' size='340' side='right'caption='[[1s58]], [[Resolution|resolution]] 3.50Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1s58]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1s58]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_parvovirus_B19 Human parvovirus B19]. The May 2010 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Parvoviruses'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2010_5 10.2210/rcsb_pdb/mom_2010_5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S58 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S58 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=1s58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s58 OCA], [https://pdbe.org/1s58 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s58 RCSB], [https://www.ebi.ac.uk/pdbsum/1s58 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s58 ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CAPSD_PAVHV CAPSD_PAVHV] Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 20 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 (PubMed:15289612). The capsid encapsulates the genomic ssDNA (Probable). Binds to erythroid progenitor cells expressing high levels of P antigen and uses host ITGA5-ITGB1 and XRCC5/Ku80 autoantigen as coreceptors on the cell surface to provide virion attachment to target cell (PubMed:12907437, PubMed:8211117, PubMed:16076874). This attachment induces virion internalization predominantly through clathrin-dependent endocytosis (PubMed:22718826). Binding to the host receptors also induces capsid rearrangements leading to surface exposure of VP1 N-terminus, specifically its phospholipase A2-like region (PubMed:17020940). The additional N-terminal region of isoform Minor capsid protein VP1, called VP1u, may serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell and might contribute to virus transport to the nucleus (PubMed:11702787).<ref>PMID:11702787</ref> <ref>PMID:12907437</ref> <ref>PMID:15289612</ref> <ref>PMID:16076874</ref> <ref>PMID:17020940</ref> <ref>PMID:22718826</ref> <ref>PMID:8211117</ref> | ||
== 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=1s58 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=1s58 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Human parvovirus B19 is the only parvovirus known to be a human pathogen. The structure of recombinant B19-like particles has been determined to approximately 3.5-A resolution by x-ray crystallography and, to our knowledge, represents the first near-atomic structure of an Erythrovirus. The polypeptide fold of the major capsid protein VP2 is a "jelly roll" with a beta-barrel motif similar to that found in many icosahedral viruses. The large loops connecting the strands of the beta-barrel form surface features that differentiate B19 from other parvoviruses. Although B19 VP2 has only 26% sequence identity to VP3 of adeno-associated virus, 72% of the C(alpha) atoms can be aligned structurally with a rms deviation of 1.8 A. Both viruses require an integrin as a coreceptor, and conserved surface features suggest a common receptor-binding region. | ||
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| - | The structure of human parvovirus B19.,Kaufmann B, Simpson AA, Rossmann MG Proc Natl Acad Sci U S A. 2004 Aug 10;101(32):11628-33. Epub 2004 Aug 2. PMID:15289612<ref>PMID:15289612</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1s58" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
| - | + | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | |
| - | *[[Virus coat | + | |
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: B19 | + | [[Category: Human parvovirus B19]] |
| + | [[Category: Large Structures]] | ||
[[Category: Parvoviruses]] | [[Category: Parvoviruses]] | ||
[[Category: RCSB PDB Molecule of the Month]] | [[Category: RCSB PDB Molecule of the Month]] | ||
| - | [[Category: Kaufmann | + | [[Category: Kaufmann B]] |
| - | [[Category: Rossmann | + | [[Category: Rossmann MG]] |
| - | [[Category: Simpson | + | [[Category: Simpson AA]] |
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Current revision
The structure of B19 parvovirus capsid
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