6sit: Difference between revisions

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 <StructureSection load='6sit' size='340' side='right'caption='[[6sit]], [[Resolution|resolution]] 4.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6sit]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SIT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6SIT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6sit]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_adenovirus_B3 Human adenovirus B3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SIT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SIT 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]] 4.5&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6qnt|6qnt]], [[6qnu|6qnu]], [[5erd|5erd]]</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=6sit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sit OCA], [http://pdbe.org/6sit PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sit RCSB], [http://www.ebi.ac.uk/pdbsum/6sit PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sit 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=6sit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sit OCA], [https://pdbe.org/6sit PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sit RCSB], [https://www.ebi.ac.uk/pdbsum/6sit PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sit ProSAT]</span></td></tr>
 </table>
-== Disease ==
-[[http://www.uniprot.org/uniprot/DSG2_HUMAN DSG2_HUMAN]] Defects in DSG2 are the cause of familial arrhythmogenic right ventricular dysplasia type 10 (ARVD10) [MIM:[http://omim.org/entry/610193 610193]]; also known as arrhythmogenic right ventricular cardiomyopathy 10 (ARVC10). ARVD is an autosomal dominant disease characterized by partial degeneration of the myocardium of the right ventricle, electrical instability, and sudden death. It is clinically defined by electrocardiographic and angiographic criteria; pathologic findings, replacement of ventricular myocardium with fatty and fibrous elements, preferentially involve the right ventricular free wall.<ref>PMID:16773573</ref> <ref>PMID:20031617</ref> <ref>PMID:19863551</ref> <ref>PMID:21062920</ref>   Genetic variations in DSG2 are the cause of susceptibility to cardiomyopathy dilated type 1BB (CMD1BB) [MIM:[http://omim.org/entry/612877 612877]]. A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.<ref>PMID:18678517</ref>
 == Function ==
-[[http://www.uniprot.org/uniprot/SPIKE_ADE03 SPIKE_ADE03]] Forms spikes that protrude from each vertex of the icosahedral capsid. Interacts with host receptor CD46 to provide virion initial attachment to target cell. Fiber proteins are shed during virus entry, when virus is still at the cell surface. Heparan sulfate might also play a role in virus binding. [[http://www.uniprot.org/uniprot/DSG2_HUMAN DSG2_HUMAN]] Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion.
+[https://www.uniprot.org/uniprot/SPIKE_ADE03 SPIKE_ADE03] Forms spikes that protrude from each vertex of the icosahedral capsid. Interacts with host receptor CD46 to provide virion initial attachment to target cell. Fiber proteins are shed during virus entry, when virus is still at the cell surface. Heparan sulfate might also play a role in virus binding.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 19: @@
 </div>
 <div class="pdbe-citations 6sit" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Cadherin 3D structures|Cadherin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Human adenovirus B3]]
 [[Category: Large Structures]]
-[[Category: Burmeister, W P]]
+[[Category: Burmeister WP]]
-[[Category: Fender, P]]
+[[Category: Fender P]]
-[[Category: Vassal-Stermann, E]]
+[[Category: Vassal-Stermann E]]
-[[Category: Cell surface glycoprotein]]
-[[Category: Desmosome]]
-[[Category: Extracellular domain]]
-[[Category: Viral protein]]
-[[Category: Virus receptor]]