5erp

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==Crystal structure of human Desmocollin-2 ectodomain fragment EC2-5==
==Crystal structure of human Desmocollin-2 ectodomain fragment EC2-5==
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<StructureSection load='5erp' size='340' side='right' caption='[[5erp]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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<StructureSection load='5erp' size='340' side='right'caption='[[5erp]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5erp]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ERP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ERP FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5erp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ERP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ERP FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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]] 2.7&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5eqx|5eqx]], [[5erd|5erd]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<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=5erp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5erp OCA], [http://pdbe.org/5erp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5erp RCSB], [http://www.ebi.ac.uk/pdbsum/5erp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5erp ProSAT]</span></td></tr>
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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=5erp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5erp OCA], [https://pdbe.org/5erp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5erp RCSB], [https://www.ebi.ac.uk/pdbsum/5erp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5erp ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/DSC2_HUMAN DSC2_HUMAN]] Familial isolated arrhythmogenic ventricular dysplasia, right dominant form;Familial isolated arrhythmogenic ventricular dysplasia, biventricular form;Familial isolated arrhythmogenic ventricular dysplasia, left dominant form. The disease is caused by mutations affecting the gene represented in this entry.
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[https://www.uniprot.org/uniprot/DSC2_HUMAN DSC2_HUMAN] Familial isolated arrhythmogenic ventricular dysplasia, right dominant form;Familial isolated arrhythmogenic ventricular dysplasia, biventricular form;Familial isolated arrhythmogenic ventricular dysplasia, left dominant form. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/DSC2_HUMAN DSC2_HUMAN]] Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. May contribute to epidermal cell positioning (stratification) by mediating differential adhesiveness between cells that express different isoforms.
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[https://www.uniprot.org/uniprot/DSC2_HUMAN DSC2_HUMAN] Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. May contribute to epidermal cell positioning (stratification) by mediating differential adhesiveness between cells that express different isoforms.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 5erp" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5erp" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Cadherin 3D structures|Cadherin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Brasch, J]]
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[[Category: Homo sapiens]]
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[[Category: Harrison, O J]]
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[[Category: Large Structures]]
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[[Category: Shapiro, L]]
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[[Category: Brasch J]]
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[[Category: Cell adhesion]]
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[[Category: Harrison OJ]]
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[[Category: Cell surface]]
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[[Category: Shapiro L]]
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[[Category: Desmosome]]
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[[Category: Extracellular cadherin domain]]
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Current revision

Crystal structure of human Desmocollin-2 ectodomain fragment EC2-5

PDB ID 5erp

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