1RY4

NMR Structure of the CRIB-PDZ module of Par-6

1RY4 の概要

• エントリーDOI: 10.2210/pdb1ry4/pdb
• NMR情報: BMRB: 6126
• 分子名称: CG5884-PA (1 entity in total)
• 機能のキーワード: pdz, crib, cdc-42, cell polarization, polarity adaptor complex, cell adhesion
• 由来する生物種: Drosophila melanogaster (fruit fly)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13759.75

構造登録者

Peterson, F.C.,Penkert, R.R.,Volkman, B.F.,Prehoda, K.E. (登録日: 2003-12-19, 公開日: 2004-03-23, 最終更新日: 2024-05-22)

主引用文献

Peterson, F.C.,Penkert, R.R.,Volkman, B.F.,Prehoda, K.E.
Cdc42 Regulates the Par-6 PDZ Domain through an Allosteric CRIB-PDZ Transition.
Mol.Cell, 13:665-676, 2004

PubMed Abstract: Regulation of protein interaction domains is required for cellular signaling dynamics. Here, we show that the PDZ protein interaction domain from the cell polarity protein Par-6 is regulated by the Rho GTPase Cdc42. Cdc42 binds to a CRIB domain adjacent to the PDZ domain, increasing the affinity of the Par-6 PDZ for its carboxy-terminal ligand by approximately 13-fold. Par-6 PDZ regulation is required for function as mutational disruption of Cdc42-Par-6 PDZ coupling leads to inactivation of Par-6 in polarized MDCK epithelial cells. Structural analysis reveals that the free PDZ domain has several deviations from the canonical PDZ conformation that account for its low ligand affinity. Regulation results from a Cdc42-induced conformational transition in the CRIB-PDZ module that causes the PDZ to assume a canonical, high-affinity PDZ conformation. The coupled CRIB and PDZ architecture of Par-6 reveals how simple binding domains can be combined to yield complex regulation.

PubMed: 15023337
DOI: 10.1016/S1097-2765(04)00086-3

実験手法

SOLUTION NMR