View source for 6mhq


==Structure of connexin-46 intercellular gap junction channel at 3.4 angstrom resolution by cryoEM==
<SX load='6mhq' size='340' side='right' viewer='molstar' caption='[[6mhq]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6mhq]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MHQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MHQ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4&#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=6mhq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mhq OCA], [https://pdbe.org/6mhq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mhq RCSB], [https://www.ebi.ac.uk/pdbsum/6mhq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mhq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CXA3_SHEEP CXA3_SHEEP] 
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== Publication Abstract from PubMed ==
Gap junctions establish direct pathways for cell-to-cell communication through the assembly of twelve connexin subunits that form intercellular channels connecting neighbouring cells. Co-assembly of different connexin isoforms produces channels with unique properties and enables communication across cell types. Here we used single-particle cryo-electron microscopy to investigate the structural basis of connexin co-assembly in native lens gap junction channels composed of connexin 46 and connexin 50 (Cx46/50). We provide the first comparative analysis to connexin 26 (Cx26), which-together with computational studies-elucidates key energetic features governing gap junction permselectivity. Cx46/50 adopts an open-state conformation that is distinct from the Cx26 crystal structure, yet it appears to be stabilized by a conserved set of hydrophobic anchoring residues. 'Hot spots' of genetic mutations linked to hereditary cataract formation map to the core structural-functional elements identified in Cx46/50, suggesting explanations for many of the disease-causing effects.

Structure of native lens connexin 46/50 intercellular channels by cryo-EM.,Myers JB, Haddad BG, O'Neill SE, Chorev DS, Yoshioka CC, Robinson CV, Zuckerman DM, Reichow SL Nature. 2018 Dec;564(7736):372-377. doi: 10.1038/s41586-018-0786-7. Epub 2018 Dec, 12. PMID:30542154<ref>PMID:30542154</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 6mhq" style="background-color:#fffaf0;"></div>

==See Also==
*[[Connexin 3D structure|Connexin 3D structure]]
== References ==
<references/>
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[[Category: Large Structures]]
[[Category: Ovis aries]]
[[Category: Myers JB]]
[[Category: Reichow SL]]