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4nuq

From Proteopedia

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Revision as of 10:50, 4 August 2016

Crystal structure of mouse N-cadherin EC1-2 W2F

Structural highlights

4nuq is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	4num, 4nup
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2]

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Cavallaro U, Niedermeyer J, Fuxa M, Christofori G. N-CAM modulates tumour-cell adhesion to matrix by inducing FGF-receptor signalling. Nat Cell Biol. 2001 Jul;3(7):650-7. PMID:11433297 doi:http://dx.doi.org/10.1038/35083041
↑ Yasuda S, Tanaka H, Sugiura H, Okamura K, Sakaguchi T, Tran U, Takemiya T, Mizoguchi A, Yagita Y, Sakurai T, De Robertis EM, Yamagata K. Activity-induced protocadherin arcadlin regulates dendritic spine number by triggering N-cadherin endocytosis via TAO2beta and p38 MAP kinases. Neuron. 2007 Nov 8;56(3):456-71. PMID:17988630 doi:http://dx.doi.org/10.1016/j.neuron.2007.08.020
↑ 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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4nuq"

Categories: Jin, X | Cell adhesion | Cell adhesion molecule

@@ Line 1: / Line 1: @@
 ==Crystal structure of mouse N-cadherin EC1-2 W2F==
 <StructureSection load='4nuq' size='340' side='right' caption='[[4nuq]], [[Resolution|resolution]] 2.12&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </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">[[4num|4num]], [[4nup|4nup]]</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=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>
+<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://pdbe.org/4nuq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nuq RCSB], [http://www.ebi.ac.uk/pdbsum/4nuq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nuq ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4nuq" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Cadherin|Cadherin]]
 == References ==
 <references/>

4nuq

From Proteopedia

Revision as of 10:50, 4 August 2016

Crystal structure of mouse N-cadherin EC1-2 W2F

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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