View source for 5ayq


==Structure-based site-directed photo-crosslinking analyses of multimeric cell-adhesive interactions of VGSC beta subunits==
<StructureSection load='5ayq' size='340' side='right'caption='[[5ayq]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ayq]] is a 2 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=5AYQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AYQ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</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=5ayq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ayq OCA], [https://pdbe.org/5ayq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ayq RCSB], [https://www.ebi.ac.uk/pdbsum/5ayq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ayq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SCN4B_MOUSE SCN4B_MOUSE] Modulates channel gating kinetics. Causes negative shifts in the voltage dependence of activation of certain alpha sodium channels, but does not affect the voltage dependence of inactivation. Modulates the suceptibility of the sodium channel to inhibition by toxic peptides from spider, scorpion, wasp and sea anemone venom (By similarity).
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== Publication Abstract from PubMed ==
The beta1, beta2, and beta4 subunits of voltage-gated sodium channels reportedly function as cell adhesion molecules. The present crystallographic analysis of the beta4 extracellular domain revealed an antiparallel arrangement of the beta4 molecules in the crystal lattice. The interface between the two antiparallel beta4 molecules is asymmetric, and results in a multimeric assembly. Structure-based mutagenesis and site-directed photo-crosslinking analyses of the beta4-mediated cell-cell adhesion revealed that the interface between the antiparallel beta4 molecules corresponds to that in the trans homophilic interaction for the multimeric assembly of beta4 in cell-cell adhesion. This trans interaction mode is also employed in the beta1-mediated cell-cell adhesion. Moreover, the beta1 gene mutations associated with generalized epilepsy with febrile seizures plus (GEFS+) impaired the beta1-mediated cell-cell adhesion, which should underlie the GEFS+ pathogenesis. Thus, the structural basis for the beta-subunit-mediated cell-cell adhesion has been established.

Structure-based site-directed photo-crosslinking analyses of multimeric cell-adhesive interactions of voltage-gated sodium channel beta subunits.,Shimizu H, Miyazaki H, Ohsawa N, Shoji S, Ishizuka-Katsura Y, Tosaki A, Oyama F, Terada T, Sakamoto K, Shirouzu M, Sekine S, Nukina N, Yokoyama S Sci Rep. 2016 May 24;6:26618. doi: 10.1038/srep26618. PMID:27216889<ref>PMID:27216889</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5ayq" style="background-color:#fffaf0;"></div>

==See Also==
*[[Ion channels 3D structures|Ion channels 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Shimizu H]]