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4nuq

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==Crystal structure of mouse N-cadherin EC1-2 W2F==
==Crystal structure of mouse N-cadherin EC1-2 W2F==
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<StructureSection load='4nuq' size='340' side='right' caption='[[4nuq]], [[Resolution|resolution]] 2.12&Aring;' scene=''>
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<StructureSection load='4nuq' size='340' side='right'caption='[[4nuq]], [[Resolution|resolution]] 2.12&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4nuq]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NUQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NUQ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4nuq]] is a 1 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=4NUQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NUQ 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=CA:CALCIUM+ION'>CA</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]] 2.116&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4num|4num]], [[4nup|4nup]]</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=CA:CALCIUM+ION'>CA</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=4nuq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nuq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nuq RCSB], [http://www.ebi.ac.uk/pdbsum/4nuq PDBsum]</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=4nuq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nuq OCA], [https://pdbe.org/4nuq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nuq RCSB], [https://www.ebi.ac.uk/pdbsum/4nuq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nuq ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/CADH2_MOUSE CADH2_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. CDH2 may be involved in neuronal recognition mechanism. In hippocampal neurons, may regulate dendritic spine density.<ref>PMID:11433297</ref> <ref>PMID:17988630</ref>
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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.
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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<ref>PMID:25253890</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
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</div>
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*[[Cadherin 3D structures|Cadherin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Jin, X.]]
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[[Category: Large Structures]]
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[[Category: Cell adhesion]]
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[[Category: Mus musculus]]
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[[Category: Cell adhesion molecule]]
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[[Category: Jin X]]

Current revision

Crystal structure of mouse N-cadherin EC1-2 W2F

PDB ID 4nuq

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