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Gap junction structure: Unraveled, but not fully revealed

F1000Research, ISSN: 1759-796X, Vol: 6, Page: 568
2017
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Review Description

Gap junction channels facilitate the intercellular exchange of ions and small molecules, a process that is critical for the function of many different kinds of cells and tissues. Recent crystal structures of channels formed by one connexin isoform (connexin26) have been determined, and they have been subjected to molecular modeling. These studies have provided high-resolution models to gain insights into the mechanisms of channel conductance, molecular permeability, and gating. The models share similarities, but there are some differences in the conclusions reached by these studies. Many unanswered questions remain to allow an atomic-level understanding of intercellular communication mediated by connexin26. Because some domains of the connexin polypeptides are highly conserved (like the transmembrane regions), it is likely that some features of the connexin26 structure will apply to other members of the family of gap junction proteins. However, determination of high-resolution structures and modeling of other connexin channels will be required to account for the diverse biophysical properties and regulation conferred by the differences in their sequences.

Bibliographic Details

Eric C. Beyer; Viviana M. Berthoud

F1000 ( Faculty of 1000 Ltd)

Biochemistry, Genetics and Molecular Biology; Immunology and Microbiology; Pharmacology, Toxicology and Pharmaceutics

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