2qku: Difference between revisions
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'''The 5th PDZ Domain of InaD in 10mM DTT''' | '''The 5th PDZ Domain of InaD in 10mM DTT''' | ||
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[[Category: Socolich, M.]] | [[Category: Socolich, M.]] | ||
[[Category: Wall, M.]] | [[Category: Wall, M.]] | ||
[[Category: | [[Category: Disulfide bond]] | ||
[[Category: | [[Category: Membrane]] | ||
[[Category: | [[Category: Pdz domain]] | ||
[[Category: | [[Category: Peptide binding protein]] | ||
[[Category: | [[Category: Scaffolding protein]] | ||
[[Category: | [[Category: Sensory transduction]] | ||
[[Category: | [[Category: Vision]] | ||
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Revision as of 12:08, 4 May 2008
The 5th PDZ Domain of InaD in 10mM DTT
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
2QKU 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 Page seeded by OCA on Sun May 4 15:08:12 2008
