2qkt
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(New page: 200px<br /><applet load="2qkt" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qkt, resolution 2.05Å" /> '''Crystal Structure of...)
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Revision as of 10:23, 23 January 2008
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Crystal Structure of the 5th PDZ domain of InaD
Overview
The INAD scaffold organizes a multiprotein complex that is essential for, proper visual signaling in Drosophila photoreceptor cells. Here we show, that one of the INAD PDZ domains (PDZ5) exists in a redox-dependent, equilibrium between two conformations--a reduced form that is similar to, the structure of other PDZ domains, and an oxidized form in which the, ligand-binding site is distorted through formation of a strong, intramolecular disulfide bond. We demonstrate transient light-dependent, formation of this disulfide bond in vivo and find that transgenic flies, expressing a mutant INAD in which PDZ5 is locked in the reduced state, display severe defects in termination of visual responses and visually, mediated reflex behavior. These studies demonstrate a conformational, switch mechanism for PDZ domain function and suggest that INAD behaves, more like a dynamic machine rather than a passive scaffold, regulating, signal transduction at the millisecond timescale through cycles of, conformational change.
About this Structure
2QKT is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.
Reference
Dynamic scaffolding in a g protein-coupled signaling system., Mishra P, Socolich M, Wall MA, Graves J, Wang Z, Ranganathan R, Cell. 2007 Oct 5;131(1):80-92. PMID:17923089
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