1fpv: Difference between revisions

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 <StructureSection load='1fpv' size='340' side='right'caption='[[1fpv]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1fpv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Fplv Fplv]. 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=1FPV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FPV FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1fpv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Feline_panleukopenia_virus Feline panleukopenia virus]. 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=1FPV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FPV FirstGlance]. <br>
-</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=1fpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fpv OCA], [https://pdbe.org/1fpv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fpv RCSB], [https://www.ebi.ac.uk/pdbsum/1fpv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fpv ProSAT]</span></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]] 3.3&#8491;</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=1fpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fpv OCA], [https://pdbe.org/1fpv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fpv RCSB], [https://www.ebi.ac.uk/pdbsum/1fpv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fpv ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/CAPSD_FPV19 CAPSD_FPV19]] 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).
+[https://www.uniprot.org/uniprot/CAPSD_FPV19 CAPSD_FPV19] 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
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    <jmolCheckbox>
      <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fp/1fpv_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>
    </jmolCheckbox>
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 __TOC__
 </StructureSection>
-[[Category: Fplv]]
+[[Category: Feline panleukopenia virus]]
 [[Category: Large Structures]]
 [[Category: Parvoviruses]]
 [[Category: RCSB PDB Molecule of the Month]]
-[[Category: Agbandje, M]]
+[[Category: Agbandje M]]
-[[Category: Rossmann, M G]]
+[[Category: Rossmann MG]]
-[[Category: Icosahedral virus]]
-[[Category: Panleukemia virus coat protein]]
-[[Category: Virus]]