4nup: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:
==Crystal structure of mouse N-cadherin EC1-2 with AA insertion between residues 2 and 3==
==Crystal structure of mouse N-cadherin EC1-2 with AA insertion between residues 2 and 3==
<StructureSection load='4nup' size='340' side='right' caption='[[4nup]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='4nup' size='340' side='right' caption='[[4nup]], [[Resolution|resolution]] 2.70&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>
</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]], [[4nuq|4nuq]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4num|4num]], [[4nuq|4nuq]]</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=4nup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nup OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nup RCSB], [http://www.ebi.ac.uk/pdbsum/4nup 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=4nup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nup OCA], [http://pdbe.org/4nup PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nup RCSB], [http://www.ebi.ac.uk/pdbsum/4nup PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nup ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
Line 17: Line 18:
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 4nup" style="background-color:#fffaf0;"></div>
==See Also==
*[[Cadherin|Cadherin]]
== References ==
== References ==
<references/>
<references/>

Revision as of 07:51, 5 August 2016

Crystal structure of mouse N-cadherin EC1-2 with AA insertion between residues 2 and 3Crystal structure of mouse N-cadherin EC1-2 with AA insertion between residues 2 and 3

Structural highlights

4nup is a 3 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[Q3UIC2_MOUSE] Cadherins are calcium dependent cell adhesion proteins (By similarity).[RuleBase:RU004357]

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

  1. 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

4nup, resolution 2.70Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA