2LA8
Solution structure of INAD PDZ5 complexed with Kon-tiki peptide
Summary for 2LA8
| Entry DOI | 10.2210/pdb2la8/pdb |
| Related | 3R0H |
| NMR Information | BMRB: 17515 |
| Descriptor | Inactivation-no-after-potential D protein,kon-tiki peptide (1 entity in total) |
| Functional Keywords | peptide binding protein |
| Biological source | Drosophila melanogaster (Fruit fly) More |
| Total number of polymer chains | 1 |
| Total formula weight | 11598.38 |
| Authors | |
| Primary citation | Liu, W.,Wen, W.,Wei, Z.,Yu, J.,Ye, F.,Liu, C.-H.,Hardie, R.C.,Zhang, M. The INAD scaffold is a dynamic, redox-regulated modulator of signaling in the Drosophila eye Cell(Cambridge,Mass.), 145:1088-1101, 2011 Cited by PubMed Abstract: 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 ∼330 mV. Acidification, potentially mediated via light and PLCβ-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. PubMed: 21703451DOI: 10.1016/j.cell.2011.05.015 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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