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| | <StructureSection load='4oy9' size='340' side='right'caption='[[4oy9]], [[Resolution|resolution]] 1.62Å' scene=''> | | <StructureSection load='4oy9' size='340' side='right'caption='[[4oy9]], [[Resolution|resolution]] 1.62Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4oy9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OY9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OY9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4oy9]] is a 1 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=4OY9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OY9 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='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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CDH3,CDHP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4oy9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oy9 OCA], [https://pdbe.org/4oy9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4oy9 RCSB], [https://www.ebi.ac.uk/pdbsum/4oy9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4oy9 ProSAT]</span></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=4oy9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oy9 OCA], [http://pdbe.org/4oy9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4oy9 RCSB], [http://www.ebi.ac.uk/pdbsum/4oy9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4oy9 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Disease == | | == 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. | + | [https://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 == | | == 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. | + | [https://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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lucarelli, A P]] | + | [[Category: Dalle Vedove A]] |
| - | [[Category: Matino, A]] | + | [[Category: Lucarelli AP]] |
| - | [[Category: Nardone, V]] | + | [[Category: Matino A]] |
| - | [[Category: Parisini, E]]
| + | [[Category: Nardone V]] |
| - | [[Category: Vedove, A Dalle]]
| + | [[Category: Parisini E]] |
| - | [[Category: Adhesion]] | + | |
| - | [[Category: Cadherin]] | + | |
| - | [[Category: Calcium-binding protein]]
| + | |
| - | [[Category: Cell adhesion]]
| + | |
| 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 PubMed
Cadherins are a large family of calcium-dependent proteins that mediate cellular adherens junction formation and tissue morphogenesis. To date, the most studied cadherins are those classified as classical, which are further divided into type I or type II depending on selected sequence features. Unlike other members of the classical cadherin family, a detailed structural characterization of P-cadherin has not yet been fully obtained. Here, the high-resolution crystal structure determination of the closed form of human P-cadherin EC1-EC2 is reported. The structure shows a novel, monomeric packing arrangement that provides a further snapshot in the yet-to-be-achieved complete description of the highly dynamic cadherin dimerization pathway. Moreover, this is the first multidomain cadherin fragment to be crystallized and structurally characterized in its closed conformation that does not carry any extra N-terminal residues before the naturally occurring aspartic acid at position 1. Finally, two clear alternate conformations are observed for the critical Trp2 residue, suggestive of a transient, metastable state. The P-cadherin structure and packing arrangement shown here provide new and valuable information towards the complete structural characterization of the still largely elusive cadherin dimerization pathway.
The X-ray structure of human P-cadherin EC1-EC2 in a closed conformation provides insight into the type I cadherin dimerization pathway.,Dalle Vedove A, Lucarelli AP, Nardone V, Matino A, Parisini E Acta Crystallogr F Struct Biol Commun. 2015 Apr;71(Pt 4):371-80. doi:, 10.1107/S2053230X15003878. Epub 2015 Mar 20. PMID:25849494[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Dalle Vedove A, Lucarelli AP, Nardone V, Matino A, Parisini E. The X-ray structure of human P-cadherin EC1-EC2 in a closed conformation provides insight into the type I cadherin dimerization pathway. Acta Crystallogr F Struct Biol Commun. 2015 Apr;71(Pt 4):371-80. doi:, 10.1107/S2053230X15003878. Epub 2015 Mar 20. PMID:25849494 doi:http://dx.doi.org/10.1107/S2053230X15003878
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