1s58: Difference between revisions

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<StructureSection load='1s58' size='340' side='right'caption='[[1s58]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
<StructureSection load='1s58' size='340' side='right'caption='[[1s58]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1s58]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/B19_virus B19 virus]. The May 2010 RCSB PDB [http://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 [http://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 [http://proteopedia.org/fgij/fg.htm?mol=1S58 FirstGlance]. <br>
<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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1k3v|1k3v]], [[1lp3|1lp3]], [[1fpv|1fpv]], [[1mvm|1mvm]], [[4dpv|4dpv]], [[1dnv|1dnv]]</div></td></tr>
</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">vp2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10798 B19 virus])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1s58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s58 OCA], [http://pdbe.org/1s58 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1s58 RCSB], [http://www.ebi.ac.uk/pdbsum/1s58 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1s58 ProSAT]</span></td></tr>
</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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==See Also==
==See Also==
*[[Canine parvovirus|Canine parvovirus]]
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
== References ==
== References ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: B19 virus]]
[[Category: Human parvovirus B19]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Parvoviruses]]
[[Category: Parvoviruses]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Kaufmann, B]]
[[Category: Kaufmann B]]
[[Category: Rossmann, M G]]
[[Category: Rossmann MG]]
[[Category: Simpson, A A]]
[[Category: Simpson AA]]
[[Category: Beta-barrel]]
[[Category: Icosahedral capsid]]
[[Category: Icosahedral virus]]
[[Category: Virus]]
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