2qkt: Difference between revisions

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==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.

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==

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[[Category: vision]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Wed Jan 23 12~~:23:27 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:40:07 2008''

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 24: / Line 24: @@
 [[Category: vision]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:23:27 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:40:07 2008''