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2qkt
From Proteopedia
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| - | [[Image:2qkt.jpg|left|200px]] | ||
| - | + | ==Crystal Structure of the 5th PDZ domain of InaD== | |
| - | + | <StructureSection load='2qkt' size='340' side='right'caption='[[2qkt]], [[Resolution|resolution]] 2.05Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2qkt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QKT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QKT FirstGlance]. <br> | |
| - | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">inaD ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr> | |
| - | | | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qkt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qkt OCA], [https://pdbe.org/2qkt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qkt RCSB], [https://www.ebi.ac.uk/pdbsum/2qkt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qkt ProSAT]</span></td></tr> |
| - | + | </table> | |
| - | + | == Function == | |
| - | ''' | + | [[https://www.uniprot.org/uniprot/INAD_DROME INAD_DROME]] Involved in the negative feedback regulation of the light-activated signaling cascade in photoreceptors through a calcium-mediated process. Interacts with tetrapeptide ligand located in C-terminal sequence of 3 key components of the visual cascade, tethering them and forming a macromolecular signaling phototransduction complex.<ref>PMID:7826638</ref> <ref>PMID:11342563</ref> |
| - | + | == Evolutionary Conservation == | |
| - | + | [[Image:Consurf_key_small.gif|200px|right]] | |
| - | == | + | Check<jmol> |
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qk/2qkt_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2qkt ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
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. | ||
| - | + | 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<ref>PMID:17923089</ref> | |
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| - | Dynamic scaffolding in a | + | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2qkt" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Drome]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Ranganathan, R]] | ||
| + | [[Category: Socolich, M]] | ||
| + | [[Category: Disulfide-bond]] | ||
| + | [[Category: Membrane]] | ||
| + | [[Category: Pdz domain]] | ||
| + | [[Category: Peptide binding protein]] | ||
| + | [[Category: Scaffolding protein]] | ||
| + | [[Category: Sensory transduction]] | ||
| + | [[Category: Signaling protein]] | ||
| + | [[Category: Vision]] | ||
Current revision
Crystal Structure of the 5th PDZ domain of InaD
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