2QKU

The 5th PDZ Domain of InaD in 10mM DTT

2QKU の概要

• エントリーDOI: 10.2210/pdb2qku/pdb
• 関連するPDBエントリー: 2QKT 2QKV
• 分子名称: Inactivation-no-after-potential D protein, GLYCEROL (3 entities in total)
• 機能のキーワード: pdz domain; scaffolding protein; disulfide bond, membrane, sensory transduction, vision, peptide binding protein
• 由来する生物種: Drosophila melanogaster (fruit fly)
• 細胞内の位置: Cell membrane; Peripheral membrane protein: Q24008
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 29599.16

構造登録者

Ranganathan, R.,Socolich, M.,Wall, M. (登録日: 2007-07-11, 公開日: 2007-11-06, 最終更新日: 2024-10-09)

主引用文献

Mishra, P.,Socolich, M.,Wall, M.A.,Graves, J.,Wang, Z.,Ranganathan, R.
Dynamic Scaffolding in a G Protein-Coupled Signaling System.
Cell(Cambridge,Mass.), 131:80-92, 2007

PubMed Abstract: 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.

PubMed: 17923089
DOI: 10.1016/j.cell.2007.07.037

実験手法

X-RAY DIFFRACTION (2.2 Å)