4nuq: Difference between revisions
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==Crystal structure of mouse N-cadherin EC1-2 W2F== | ==Crystal structure of mouse N-cadherin EC1-2 W2F== | ||
<StructureSection load='4nuq' size='340' side='right' caption='[[4nuq]], [[Resolution|resolution]] 2.12Å' scene=''> | <StructureSection load='4nuq' size='340' side='right'caption='[[4nuq]], [[Resolution|resolution]] 2.12Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<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> | <table><tr><td colspan='2'>[[4nuq]] is a 1 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=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> | ||
</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">[[4num|4num]], [[4nup|4nup]]</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cdh2 ([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=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> | <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> | </table> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Lk3 transgenic mice]] | |||
[[Category: Jin, X]] | [[Category: Jin, X]] | ||
[[Category: Cell adhesion]] | [[Category: Cell adhesion]] | ||
[[Category: Cell adhesion molecule]] | [[Category: Cell adhesion molecule]] | ||
Revision as of 12:06, 10 April 2019
Crystal structure of mouse N-cadherin EC1-2 W2FCrystal structure of mouse N-cadherin EC1-2 W2F
Structural highlights
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 PubMedType 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. See AlsoReferences
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