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2qkv

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(New page: 200px<br /><applet load="2qkv" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qkv, resolution 1.550&Aring;" /> '''Crystal Structure o...)
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==Overview==
==Overview==
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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.
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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==
==About this Structure==
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[[Category: vision]]
[[Category: vision]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:23:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:40:06 2008''

Revision as of 16:40, 21 February 2008


2qkv, resolution 1.550Å

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Crystal Structure of the C645S Mutant 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

2QKV 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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