1p1e
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(New page: 200px<br /><applet load="1p1e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p1e" /> '''Structural Insights into the Inter-domain Ch...)
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Revision as of 21:15, 20 November 2007
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Structural Insights into the Inter-domain Chaperoning of Tandem PDZ Domains in Glutamate Receptor Interacting Proteins
Overview
The interaction of the glutamate receptor subunits 2 and 3 (GluR2/3) with, multi-PDZ domain glutamate receptor-interacting protein (GRIP) is, important for the synaptic trafficking and clustering of the receptors., Binding of GluR2/3 to GRIP requires both the fourth and fifth PDZ domains, (PDZ4 and PDZ5) to be covalently linked, although only one PDZ domain is, directly involved in binding to the receptor tail. To elucidate the, molecular basis of this mode of PDZ domain-mediated target recognition, we, solved the solution structures of the PDZ45 tandem and the isolated PDZ4, of GRIP. The two PDZ domains form a compact structure with a fixed, interdomain orientation. The interdomain packing and the stable folding of, both PDZ domains require a short stretch of amino acids N-terminal to PDZ4, and a conserved linker connecting PDZ4 and PDZ5. PDZ4 contains a deformed, aB-bB groove that is unlikely to bind to carboxyl peptides. Instead, the, domain stabilizes the structure of PDZ5.
About this Structure
1P1E is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Tandem PDZ repeats in glutamate receptor-interacting proteins have a novel mode of PDZ domain-mediated target binding., Feng W, Shi Y, Li M, Zhang M, Nat Struct Biol. 2003 Nov;10(11):972-8. Epub 2003 Oct 12. PMID:14555997
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