6cgu: Difference between revisions
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<StructureSection load='6cgu' size='340' side='right' caption='[[6cgu]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='6cgu' size='340' side='right' caption='[[6cgu]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6cgu]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CGU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CGU FirstGlance]. <br> | <table><tr><td colspan='2'>[[6cgu]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CGU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CGU 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"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6cg6|6cg6]], [[6cg7|6cg7]], [[6cgb|6cgb]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6cg6|6cg6]], [[6cg7|6cg7]], [[6cgb|6cgb]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cdh6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=6cgu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cgu OCA], [http://pdbe.org/6cgu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cgu RCSB], [http://www.ebi.ac.uk/pdbsum/6cgu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cgu 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=6cgu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cgu OCA], [http://pdbe.org/6cgu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cgu RCSB], [http://www.ebi.ac.uk/pdbsum/6cgu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cgu ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/CADH6_MOUSE CADH6_MOUSE]] 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. | [[http://www.uniprot.org/uniprot/CADH6_MOUSE CADH6_MOUSE]] 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 == | |||
Type II cadherins are cell-cell adhesion proteins critical for tissue patterning and neuronal targeting but whose molecular binding code remains poorly understood. Here, we delineate binding preferences for type II cadherin cell-adhesive regions, revealing extensive heterophilic interactions between specific pairs, in addition to homophilic interactions. Three distinct specificity groups emerge from our analysis with members that share highly similar heterophilic binding patterns and favor binding to one another. Structures of adhesive fragments from each specificity group confirm near-identical dimer topology conserved throughout the family, allowing interface residues whose conservation corresponds to specificity preferences to be identified. We show that targeted mutation of these residues converts binding preferences between specificity groups in biophysical and co-culture assays. Our results provide a detailed understanding of the type II cadherin interaction map and a basis for defining their role in tissue patterning and for the emerging importance of their heterophilic interactions in neural connectivity. | |||
Homophilic and Heterophilic Interactions of Type II Cadherins Identify Specificity Groups Underlying Cell-Adhesive Behavior.,Brasch J, Katsamba PS, Harrison OJ, Ahlsen G, Troyanovsky RB, Indra I, Kaczynska A, Kaeser B, Troyanovsky S, Honig B, Shapiro L Cell Rep. 2018 May 8;23(6):1840-1852. doi: 10.1016/j.celrep.2018.04.012. PMID:29742438<ref>PMID:29742438</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6cgu" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Lk3 transgenic mice]] | |||
[[Category: Brasch, J]] | [[Category: Brasch, J]] | ||
[[Category: Harrison, O J]] | [[Category: Harrison, O J]] | ||
Revision as of 10:46, 23 May 2018
mouse cadherin-6 EC1-2 adhesive fragmentmouse cadherin-6 EC1-2 adhesive fragment
Structural highlights
Function[CADH6_MOUSE] 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 PubMedType II cadherins are cell-cell adhesion proteins critical for tissue patterning and neuronal targeting but whose molecular binding code remains poorly understood. Here, we delineate binding preferences for type II cadherin cell-adhesive regions, revealing extensive heterophilic interactions between specific pairs, in addition to homophilic interactions. Three distinct specificity groups emerge from our analysis with members that share highly similar heterophilic binding patterns and favor binding to one another. Structures of adhesive fragments from each specificity group confirm near-identical dimer topology conserved throughout the family, allowing interface residues whose conservation corresponds to specificity preferences to be identified. We show that targeted mutation of these residues converts binding preferences between specificity groups in biophysical and co-culture assays. Our results provide a detailed understanding of the type II cadherin interaction map and a basis for defining their role in tissue patterning and for the emerging importance of their heterophilic interactions in neural connectivity. Homophilic and Heterophilic Interactions of Type II Cadherins Identify Specificity Groups Underlying Cell-Adhesive Behavior.,Brasch J, Katsamba PS, Harrison OJ, Ahlsen G, Troyanovsky RB, Indra I, Kaczynska A, Kaeser B, Troyanovsky S, Honig B, Shapiro L Cell Rep. 2018 May 8;23(6):1840-1852. doi: 10.1016/j.celrep.2018.04.012. PMID:29742438[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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