Crucial motifs and residues in the extracellular loops influence the formation and specificity of connexin docking.

摘要: Most of the early studies on gap junction (GJ) channel function and docking compatibility were rodent connexins, while recent research GJ channels gradually shifted from to human connexins largely due fact that mutations in many connexin genes are found associate with inherited diseases. The have revealed some key differences those rodents, calling for a comprehensive characterization channels. Functional formation functional between two hemichannels possible only docking-compatible connexins. Two groups been identified. Compatibility is believed be their amino acid residue at extracellular loop domains (E1 E2). Sequence alignment E1 E2 all known make GJs they highly conserved show high sequence identity Cx26, which near atomic resolution structure. We hypothesize different similar structure as Cx26 use corresponding residues docking. Based analysis well-studied we propose E1-E1 interactions staggered each interacting E1s docked connexon. putative both -incompatible indicating does not likely serve role compatibility. However, case E2-E2 interactions, within suggesting Docking attracted lot attention mutational hotspots several connexin-linked This article part Special Issue entitled: Gap Junction Proteins edited by Jean Claude Herve.