1txh

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{{Theoretical_model}}
{{Theoretical_model}}
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[[Image:1txh.png|left|200px]]
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==A THEORETICAL C-ALPHA MODEL OF THE TRANSMEMBRANE ALPHA- HELICES IN GAP JUNCTION INTERCELLULAR CHANNELS==
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<StructureSection load='1txh' size='340' side='right'caption='[[1txh]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TXH FirstGlance]. <br>
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</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=1txh FirstGlance], [https://www.ebi.ac.uk/pdbsum/1txh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1txh ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Gap junction channels connect the cytoplasms of apposed cells via an intercellular conduit formed by the end-to-end docking of two hexameric hemichannels called connexons. We used electron cryomicroscopy to derive a three-dimensional density map at 5.7 angstroms in-plane and 19.8 angstroms vertical resolution, allowing us to identify the positions and tilt angles for the 24 alpha helices within each hemichannel. The four hydrophobic segments in connexin sequences were assigned to the alpha helices in the map based on biochemical and phylogenetic data. Analyses of evolutionary conservation and compensatory mutations in connexin evolution identified the packing interfaces between the helices. The final model, which specifies the coordinates of Calpha atoms in the transmembrane domain, provides a structural basis for understanding the different physiological effects of almost 30 mutations and polymorphisms in terms of structural deformations at the interfaces between helices, revealing an intimate connection between molecular structure and disease.
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{{STRUCTURE_1txh| PDB=1txh | SCENE= }}
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A Calpha model for the transmembrane alpha helices of gap junction intercellular channels.,Fleishman SJ, Unger VM, Yeager M, Ben-Tal N Mol Cell. 2004 Sep 24;15(6):879-88. PMID:15383278<ref>PMID:15383278</ref>
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===A THEORETICAL C-ALPHA MODEL OF THE TRANSMEMBRANE ALPHA- HELICES IN GAP JUNCTION INTERCELLULAR CHANNELS===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_15383278}}
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<div class="pdbe-citations 1txh" style="background-color:#fffaf0;"></div>
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:015383278</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
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[[Category: Theoretical Model]]
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[[Category: Large Structures]]
[[Category: Ben-Tal, N]]
[[Category: Ben-Tal, N]]
[[Category: Fleishman, S J]]
[[Category: Fleishman, S J]]
[[Category: Unger, V M]]
[[Category: Unger, V M]]
[[Category: Yeager, M]]
[[Category: Yeager, M]]

Current revision

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

A THEORETICAL C-ALPHA MODEL OF THE TRANSMEMBRANE ALPHA- HELICES IN GAP JUNCTION INTERCELLULAR CHANNELS

PDB ID 1txh

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