Domain-swapped dimerization of ZO-1 PDZ2 generates specific and regulatory connexin43-binding sites.

ABSTRACT: PDZ domain scaffold proteins are capable of assembling macromolecular protein complexes in diverse cellular processes through PDZ-mediated binding to a short peptide fragment at the carboxyl tail of target proteins. How each PDZ domain specifically recognizes its target protein(s) remains a major conceptual question, as at least a few out of the several hundred PDZ domains in each eukaryotic genome share overlapping binding properties with any given target protein. Here, we show that the domain-swapped dimerization of zonula occludens-1 PDZ2 generates a distinct interface that functions together with the well-separated canonical carboxyl tail-binding pocket in each PDZ unit in binding to connexin43 (Cx43). We further demonstrate that the charge-charge interaction network formed by residues

SUBMITTER: Chen J 

PROVIDER: S-EPMC2516886 | biostudies-literature | 2008 Aug

REPOSITORIES: biostudies-literature