1c8h: Difference between revisions

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<StructureSection load='1c8h' size='340' side='right'caption='[[1c8h]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
<StructureSection load='1c8h' size='340' side='right'caption='[[1c8h]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1c8h]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Canine_parvovirus Canine parvovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C8H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C8H FirstGlance]. <br>
<table><tr><td colspan='2'>[[1c8h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Canine_parvovirus Canine parvovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C8H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C8H FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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]] 3.5&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ijs|1ijs]], [[4dpv|4dpv]], [[2cas|2cas]], [[1fpv|1fpv]], [[1mvm|1mvm]], [[1c8d|1c8d]], [[1c8e|1c8e]], [[1c8f|1c8f]], [[1c8g|1c8g]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c8h OCA], [http://pdbe.org/1c8h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1c8h RCSB], [http://www.ebi.ac.uk/pdbsum/1c8h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1c8h ProSAT]</span></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=1c8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c8h OCA], [https://pdbe.org/1c8h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c8h RCSB], [https://www.ebi.ac.uk/pdbsum/1c8h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c8h ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CAPSD_PAVCD CAPSD_PAVCD] 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 receptor TFRC. This attachment induces virion internalization predominantly through clathrin-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 nuclear localization signal(s). VP1 N-terminus might serve as a lipolytic enzyme to breach the endosomal membrane during entry into host cell (By similarity). Intracytoplasmic transport involves microtubules and interaction between capsid proteins and host dynein. Exposure of nuclear localization signal probably allows nuclear import of capsids.<ref>PMID:11799183</ref> <ref>PMID:12970411</ref> <ref>PMID:19656887</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c8/1c8h_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c8/1c8h_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
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==See Also==
==See Also==
*[[Canine parvovirus|Canine parvovirus]]
*[[Canine parvovirus|Canine parvovirus]]
*[[Virus coat protein|Virus coat protein]]
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
== References ==
== References ==
<references/>
<references/>
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[[Category: Canine parvovirus]]
[[Category: Canine parvovirus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Rossmann, M G]]
[[Category: Rossmann MG]]
[[Category: Simpson, A A]]
[[Category: Simpson AA]]
[[Category: Beta barrel]]
[[Category: Icosahedral symmetry]]
[[Category: Icosahedral virus]]
[[Category: Viral capsid]]
[[Category: Virus]]

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