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2la8

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Revision as of 19:19, 1 August 2018

Solution structure of INAD PDZ5 complexed with Kon-tiki peptide

Structural highlights

2la8 is a 1 chain structure with sequence from Drome. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	3r0h
Gene:	inaD, CG3504 (DROME)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

Publication Abstract from PubMed

INAD is a scaffolding protein that regulates signaling in Drosophila photoreceptors. One of its PDZ domains, PDZ5, cycles between reduced and oxidized forms in response to light, but it is unclear how light affects its redox potential. Through biochemical and structural studies, we show that the redox potential of PDZ5 is allosterically regulated by its interaction with another INAD domain, PDZ4. Whereas isolated PDZ5 is stable in the oxidized state, formation of a PDZ45 "supramodule" locks PDZ5 in the reduced state by raising the redox potential of its Cys606/Cys645 disulfide bond by approximately 330 mV. Acidification, potentially mediated via light and PLCbeta-mediated hydrolysis of PIP(2), disrupts the interaction between PDZ4 and PDZ5, leading to PDZ5 oxidation and dissociation from the TRP Ca(2+) channel, a key component of fly visual signaling. These results show that scaffolding proteins can actively modulate the intrinsic redox potentials of their disulfide bonds to exert regulatory roles in signaling.

The INAD scaffold is a dynamic, redox-regulated modulator of signaling in the Drosophila eye.,Liu W, Wen W, Wei Z, Yu J, Ye F, Liu CH, Hardie RC, Zhang M Cell. 2011 Jun 24;145(7):1088-101. PMID:21703451^[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
↑ Liu W, Wen W, Wei Z, Yu J, Ye F, Liu CH, Hardie RC, Zhang M. The INAD scaffold is a dynamic, redox-regulated modulator of signaling in the Drosophila eye. Cell. 2011 Jun 24;145(7):1088-101. PMID:21703451 doi:10.1016/j.cell.2011.05.015

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2la8"

Categories: Drome | Wen, W | Zhang, M | Peptide binding protein

@@ Line 1: / Line 1: @@
 ==Solution structure of INAD PDZ5 complexed with Kon-tiki peptide==
 <StructureSection load='2la8' size='340' side='right' caption='[[2la8]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3r0h|3r0h]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">inaD, CG3504 ([http://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=2la8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2la8 OCA], [http://pdbe.org/2la8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2la8 RCSB], [http://www.ebi.ac.uk/pdbsum/2la8 PDBsum]</span></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=2la8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2la8 OCA], [http://pdbe.org/2la8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2la8 RCSB], [http://www.ebi.ac.uk/pdbsum/2la8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2la8 ProSAT]</span></td></tr>
 </table>
 == Function ==

2la8

From Proteopedia

Revision as of 19:19, 1 August 2018

Solution structure of INAD PDZ5 complexed with Kon-tiki peptide

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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