2xgk: Difference between revisions

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-==VIRUS LIKE PARTICLE OF L172W MUTANT OF MINUTE VIRUS OF MICE - THE IMMUNOSUPPRESSIVE STRAIN==
-<StructureSection load='2xgk' size='340' side='right' caption='[[2xgk]], [[Resolution|resolution]] 4.20&Aring;' scene=''>
+==Virus like particle of L172W mutant of Minute Virus of Mice - the immunosuppressive strain==
+<StructureSection load='2xgk' size='340' side='right'caption='[[2xgk]], [[Resolution|resolution]] 4.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2xgk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Minute_virus_of_mice Minute virus of mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XGK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XGK FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2xgk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Murine_minute_virus_(STRAIN_MVMI) Murine minute virus (STRAIN MVMI)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XGK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XGK FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mvm|1mvm]], [[1z1c|1z1c]]</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]] 4.2&#8491;</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=2xgk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xgk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xgk RCSB], [http://www.ebi.ac.uk/pdbsum/2xgk PDBsum]</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=2xgk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xgk OCA], [https://pdbe.org/2xgk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xgk RCSB], [https://www.ebi.ac.uk/pdbsum/2xgk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xgk ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/COAT_MUMIM COAT_MUMIM]] 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_MUMIM CAPSD_MUMIM] 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).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 16: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2xgk" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Virus coat protein|Virus coat protein]]
+*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Minute virus of mice]]
+[[Category: Large Structures]]
-[[Category: Abramo, A D]]
+[[Category: Cotmore S]]
-[[Category: Cotmore, S]]
+[[Category: D'Abramo A]]
-[[Category: Farr, G]]
+[[Category: Farr G]]
-[[Category: Hafenstein, S]]
+[[Category: Hafenstein S]]
-[[Category: Plevka, P]]
+[[Category: Plevka P]]
-[[Category: Rossmann, M G]]
+[[Category: Rossmann MG]]
-[[Category: Tattersall, P]]
+[[Category: Tattersall P]]
-[[Category: Parvovirus]]
-[[Category: Virus]]
-[[Category: Vlp]]