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The entry | ==Crystal structure of human P-cadherin (ss-dimer)== | ||
<StructureSection load='4zml' size='340' side='right' caption='[[4zml]], [[Resolution|resolution]] 1.85Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4zml]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZML OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZML 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>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4zmn|4zmn]], [[4zmo|4zmo]], [[4zmp|4zmp]], [[4zmq|4zmq]], [[4zmt|4zmt]], [[4zmv|4zmv]], [[4zmw|4zmw]], [[4zmx|4zmx]], [[4zmy|4zmy]], [[4zmz|4zmz]]</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=4zml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zml OCA], [http://pdbe.org/4zml PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zml RCSB], [http://www.ebi.ac.uk/pdbsum/4zml PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zml ProSAT]</span></td></tr> | |||
</table> | |||
== Disease == | |||
[[http://www.uniprot.org/uniprot/CADH3_HUMAN CADH3_HUMAN]] Hypotrichosis with juvenile macular degeneration;EEM syndrome. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/CADH3_HUMAN CADH3_HUMAN]] Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Orderly assembly of classical cadherins governs cell adhesion and tissue maintenance. A key event is the strand-swap dimerization of the extracellular ectodomains of two cadherin molecules from apposing cells. Here we have determined crystal structures of P-cadherin in six different conformational states to elaborate a motion picture of its adhesive dimerization at the atomic level. The snapshots revealed that cell-adhesive dimerization is facilitated by several intermediate states collectively termed X-dimer in analogy to other classical cadherins. Based on previous studies and on the combined structural, kinetic, thermodynamic, biochemical, and cellular data reported herein, we propose that the adhesive dimerization of human P-cadherin is achieved by a stepwise mechanism analogous to that of assembly chaperones. This mechanism, applicable to type I classical cadherins, confers high specificity and fast association rates. We expect these findings to guide innovative therapeutic approaches targeting P-cadherin in cancer. | |||
Adhesive Dimerization of Human P-Cadherin Catalyzed by a Chaperone-like Mechanism.,Kudo S, Caaveiro JM, Tsumoto K Structure. 2016 Sep 6;24(9):1523-1536. doi: 10.1016/j.str.2016.07.002. Epub 2016 , Aug 18. PMID:27545624<ref>PMID:27545624</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 4zml" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Caaveiro, J M.M]] | |||
[[Category: Kudo, S]] | |||
[[Category: Tsumoto, K]] | |||
[[Category: Cell adhesion]] | |||
[[Category: Conformational change]] | |||
[[Category: Dimerization]] | |||
Revision as of 00:00, 11 September 2016
Crystal structure of human P-cadherin (ss-dimer)Crystal structure of human P-cadherin (ss-dimer)
Structural highlights
Disease[CADH3_HUMAN] Hypotrichosis with juvenile macular degeneration;EEM syndrome. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. Function[CADH3_HUMAN] Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. Publication Abstract from PubMedOrderly assembly of classical cadherins governs cell adhesion and tissue maintenance. A key event is the strand-swap dimerization of the extracellular ectodomains of two cadherin molecules from apposing cells. Here we have determined crystal structures of P-cadherin in six different conformational states to elaborate a motion picture of its adhesive dimerization at the atomic level. The snapshots revealed that cell-adhesive dimerization is facilitated by several intermediate states collectively termed X-dimer in analogy to other classical cadherins. Based on previous studies and on the combined structural, kinetic, thermodynamic, biochemical, and cellular data reported herein, we propose that the adhesive dimerization of human P-cadherin is achieved by a stepwise mechanism analogous to that of assembly chaperones. This mechanism, applicable to type I classical cadherins, confers high specificity and fast association rates. We expect these findings to guide innovative therapeutic approaches targeting P-cadherin in cancer. Adhesive Dimerization of Human P-Cadherin Catalyzed by a Chaperone-like Mechanism.,Kudo S, Caaveiro JM, Tsumoto K Structure. 2016 Sep 6;24(9):1523-1536. doi: 10.1016/j.str.2016.07.002. Epub 2016 , Aug 18. PMID:27545624[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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