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| | ==Crystal structure of mouse P-cadherin extracellular domains EC1-EC2== | | ==Crystal structure of mouse P-cadherin extracellular domains EC1-EC2== |
| - | <StructureSection load='4nqq' size='340' side='right' caption='[[4nqq]], [[Resolution|resolution]] 3.20Å' scene=''> | + | <StructureSection load='4nqq' size='340' side='right'caption='[[4nqq]], [[Resolution|resolution]] 3.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4nqq]] 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=4NQQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NQQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4nqq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NQQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NQQ 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=CU:COPPER+(II)+ION'>CU</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>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</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=10090 LK3 transgenic mice])</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=4nqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nqq OCA], [https://pdbe.org/4nqq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nqq RCSB], [https://www.ebi.ac.uk/pdbsum/4nqq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nqq 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=4nqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nqq OCA], [http://pdbe.org/4nqq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nqq RCSB], [http://www.ebi.ac.uk/pdbsum/4nqq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nqq ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CADH3_MOUSE CADH3_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. | + | [https://www.uniprot.org/uniprot/CADH3_MOUSE CADH3_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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4nqq" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4nqq" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Cadherin 3D structures|Cadherin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
| - | [[Category: Brasch, J]] | + | [[Category: Mus musculus]] |
| - | [[Category: Shapiro, L]] | + | [[Category: Brasch J]] |
| - | [[Category: Cell adhesion]] | + | [[Category: Shapiro L]] |
| - | [[Category: Cell-cell adhesion]]
| + | |
| Structural highlights
Function
CADH3_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 PubMed
Type I cadherin cell-adhesion proteins are similar in sequence and structure and yet are different enough to mediate highly specific cell-cell recognition phenomena. It has previously been shown that small differences in the homophilic and heterophilic binding affinities of different type I family members can account for the differential cell-sorting behavior. Here we use a combination of X-ray crystallography, analytical ultracentrifugation, surface plasmon resonance and double electron-electron resonance (DEER) electron paramagnetic resonance spectroscopy to identify the molecular determinants of type I cadherin dimerization affinities. Small changes in sequence are found to produce subtle structural and dynamical changes that impact relative affinities, in part via electrostatic and hydrophobic interactions, and in part through entropic effects because of increased conformational heterogeneity in the bound states as revealed by DEER distance mapping in the dimers. These findings highlight the remarkable ability of evolution to exploit a wide range of molecular properties to produce closely related members of the same protein family that have affinity differences finely tuned to mediate their biological roles.
Structural and energetic determinants of adhesive binding specificity in type I cadherins.,Vendome J, Felsovalyi K, Song H, Yang Z, Jin X, Brasch J, Harrison OJ, Ahlsen G, Bahna F, Kaczynska A, Katsamba PS, Edmond D, Hubbell WL, Shapiro L, Honig B Proc Natl Acad Sci U S A. 2014 Oct 7;111(40):E4175-84. doi:, 10.1073/pnas.1416737111. Epub 2014 Sep 24. PMID:25253890[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Vendome J, Felsovalyi K, Song H, Yang Z, Jin X, Brasch J, Harrison OJ, Ahlsen G, Bahna F, Kaczynska A, Katsamba PS, Edmond D, Hubbell WL, Shapiro L, Honig B. Structural and energetic determinants of adhesive binding specificity in type I cadherins. Proc Natl Acad Sci U S A. 2014 Oct 7;111(40):E4175-84. doi:, 10.1073/pnas.1416737111. Epub 2014 Sep 24. PMID:25253890 doi:http://dx.doi.org/10.1073/pnas.1416737111
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