1s58

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[[Image:1s58.jpg|left|200px]]
 
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{{Structure
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==The structure of B19 parvovirus capsid==
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|PDB= 1s58 |SIZE=350|CAPTION= <scene name='initialview01'>1s58</scene>, resolution 3.5&Aring;
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<StructureSection load='1s58' size='340' side='right'caption='[[1s58]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<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>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5&#8491;</td></tr>
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|GENE= vp2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10798 Human parvovirus B19])
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<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>
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}}
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/s5/1s58_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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].
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<div style="clear:both"></div>
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'''The structure of B19 parvovirus capsid'''
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==See Also==
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*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
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== References ==
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==Overview==
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<references/>
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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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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Human parvovirus B19]]
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1S58 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Human_parvovirus_b19 Human parvovirus b19]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S58 OCA].
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[[Category: Large Structures]]
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[[Category: Parvoviruses]]
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==Reference==
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[[Category: RCSB PDB Molecule of the Month]]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15289612 15289612]
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[[Category: Kaufmann B]]
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[[Category: Human parvovirus b19]]
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[[Category: Rossmann MG]]
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[[Category: Protein complex]]
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[[Category: Simpson AA]]
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[[Category: Kaufmann, B.]]
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[[Category: Rossmann, M G.]]
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[[Category: Simpson, A A.]]
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[[Category: beta-barrel]]
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[[Category: icosahedral capsid]]
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[[Category: icosahedral virus]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:00:38 2008''
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Current revision

The structure of B19 parvovirus capsid

PDB ID 1s58

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