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| | ==Crystal Structure of the 5th PDZ domain of InaD== | | ==Crystal Structure of the 5th PDZ domain of InaD== |
| - | <StructureSection load='2qkt' size='340' side='right' caption='[[2qkt]], [[Resolution|resolution]] 2.05Å' scene=''> | + | <StructureSection load='2qkt' size='340' side='right'caption='[[2qkt]], [[Resolution|resolution]] 2.05Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2qkt]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2QKT FirstGlance]. <br> | + | <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 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr> | + | </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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qkt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qkt OCA], [http://pdbe.org/2qkt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qkt RCSB], [http://www.ebi.ac.uk/pdbsum/2qkt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2qkt ProSAT]</span></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> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> | + | [[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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Drome]] | | [[Category: Drome]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Ranganathan, R]] | | [[Category: Ranganathan, R]] |
| | [[Category: Socolich, M]] | | [[Category: Socolich, M]] |
| Structural highlights
Function
[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.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Shieh BH, Niemeyer B. A novel protein encoded by the InaD gene regulates recovery of visual transduction in Drosophila. Neuron. 1995 Jan;14(1):201-10. PMID:7826638
- ↑ Kumar R, Shieh BH. The second PDZ domain of INAD is a type I domain involved in binding to eye protein kinase C. Mutational analysis and naturally occurring variants. J Biol Chem. 2001 Jul 6;276(27):24971-7. Epub 2001 May 7. PMID:11342563 doi:http://dx.doi.org/10.1074/jbc.M103570200
- ↑ Mishra P, Socolich M, Wall MA, Graves J, Wang Z, Ranganathan R. Dynamic scaffolding in a G protein-coupled signaling system. Cell. 2007 Oct 5;131(1):80-92. PMID:17923089 doi:10.1016/j.cell.2007.07.037
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