1EJ5

SOLUTION STRUCTURE OF THE AUTOINHIBITED CONFORMATION OF WASP

1EJ5 の概要

• エントリーDOI: 10.2210/pdb1ej5/pdb
• 関連するPDBエントリー: 1CEE
• 分子名称: WISKOTT-ALDRICH SYNDROME PROTEIN (1 entity in total)
• 機能のキーワード: alpha helix, beta-hairpin turn, blood clotting
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11603.60

構造登録者

Kim, A.S.,Kakalis, L.T.,Abdul-Manan, N.,Liu, G.A.,Rosen, M.K. (登録日: 2000-02-29, 公開日: 2000-04-05, 最終更新日: 2024-05-22)

主引用文献

Kim, A.S.,Kakalis, L.T.,Abdul-Manan, N.,Liu, G.A.,Rosen, M.K.
Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein.
Nature, 404:151-158, 2000

PubMed Abstract: The Rho-family GTPase, Cdc42, can regulate the actin cytoskeleton through activation of Wiskott-Aldrich syndrome protein (WASP) family members. Activation relieves an autoinhibitory contact between the GTPase-binding domain and the carboxy-terminal region of WASP proteins. Here we report the autoinhibited structure of the GTPase-binding domain of WASP, which can be induced by the C-terminal region or by organic co-solvents. In the autoinhibited complex, intramolecular interactions with the GTPase-binding domain occlude residues of the C terminus that regulate the Arp2/3 actin-nucleating complex. Binding of Cdc42 to the GTPase-binding domain causes a dramatic conformational change, resulting in disruption of the hydrophobic core and release of the C terminus, enabling its interaction with the actin regulatory machinery. These data show that 'intrinsically unstructured' peptides such as the GTPase-binding domain of WASP can be induced into distinct structural and functional states depending on context.

PubMed: 10724160
DOI: 10.1038/35010088

実験手法

SOLUTION NMR