2rcz
From Proteopedia
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Structure of the second PDZ domain of ZO-1
Overview
ZO-1 is a multidomain protein involved in cell-cell junctions and contains, three PDZ domains, which are necessary for its function in vivo. PDZ, domains play a central role in assembling diverse protein complexes, through their ability to recognize short peptide motifs on other proteins., We determined the structure of the second of the three PDZ domains of, ZO-1, which is known to promote dimerization as well as bind to C-terminal, sequences on connexins. The dimer is stabilized by extensive symmetrical, domain swapping of beta-strands, which is unlike any other known mechanism, of PDZ dimerization. The canonical peptide-binding groove remains intact, in both subunits of the PDZ2 dimer and is created by elements contributed, from both monomers. This unique structure reveals an additional example of, how PDZ domains dimerize and has multiple implications for both peptide, binding and oligomerization in vivo.
About this Structure
2RCZ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Domain swapping within PDZ2 is responsible for dimerization of ZO proteins., Fanning AS, Lye MF, Anderson JM, Lavie A, J Biol Chem. 2007 Dec 28;282(52):37710-6. Epub 2007 Oct 9. PMID:17928286
Page seeded by OCA on Wed Feb 13 08:13:26 2008
