2la8
From Proteopedia
(Difference between revisions)
| (7 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| + | |||
==Solution structure of INAD PDZ5 complexed with Kon-tiki peptide== | ==Solution structure of INAD PDZ5 complexed with Kon-tiki peptide== | ||
| - | <StructureSection load='2la8' size='340' side='right' caption='[[2la8 | + | <StructureSection load='2la8' size='340' side='right'caption='[[2la8]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | [[2la8]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2la8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LA8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LA8 FirstGlance]. <br> |
| - | <b> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2la8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2la8 OCA], [https://pdbe.org/2la8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2la8 RCSB], [https://www.ebi.ac.uk/pdbsum/2la8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2la8 ProSAT]</span></td></tr> |
| - | <b>Resources:</b> <span class='plainlinks'>[ | + | </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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == 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. | 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. | ||
| Line 11: | Line 15: | ||
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<ref>PMID:21703451</ref> | 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<ref>PMID:21703451</ref> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| + | </div> | ||
| + | <div class="pdbe-citations 2la8" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Drosophila melanogaster]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Wen W]] |
| - | [[Category: | + | [[Category: Zhang M]] |
Current revision
Solution structure of INAD PDZ5 complexed with Kon-tiki peptide
| |||||||||||
