2ADZ

solution structure of the joined PH domain of alpha1-syntrophin

2ADZ の概要

• エントリーDOI: 10.2210/pdb2adz/pdb
• 関連するPDBエントリー: 1z87
• NMR情報: BMRB: 6753
• 分子名称: Alpha-1-syntrophin (1 entity in total)
• 機能のキーワード: protein binding
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Cell membrane, sarcolemma; Peripheral membrane protein; Cytoplasmic side: Q61234
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18635.73

構造登録者

Yan, J.,Wen, W.,Xu, W.,Long, J.F.,Adams, M.E.,Froehner, S.C.,Zhang, M. (登録日: 2005-07-21, 公開日: 2006-01-24, 最終更新日: 2024-05-29)

主引用文献

Yan, J.,Wen, W.,Xu, W.,Long, J.F.,Adams, M.E.,Froehner, S.C.,Zhang, M.
Structure of the split PH domain and distinct lipid-binding properties of the PH-PDZ supramodule of alpha-syntrophin
Embo J., 24:3985-3995, 2005

PubMed Abstract: Pleckstrin homology (PH) domains play diverse roles in cytoskeletal dynamics and signal transduction. Split PH domains represent a unique subclass of PH domains that have been implicated in interactions with complementary partial PH domains 'hidden' in many proteins. Whether partial PH domains exist as independent structural units alone and whether two halves of a split PH domain can fold together to form an intact PH domain are not known. Here, we solved the structure of the PH(N)-PDZ-PH(C) tandem of alpha-syntrophin. The split PH domain of alpha-syntrophin adopts a canonical PH domain fold. The isolated partial PH domains of alpha-syntrophin, although completely unfolded, remain soluble in solution. Mixing of the two isolated domains induces de novo folding and yields a stable PH domain. Our results demonstrate that two complementary partial PH domains are capable of binding to each other to form an intact PH domain. We further showed that the PH(N)-PDZ-PH(C) tandem forms a functionally distinct supramodule, in which the split PH domain and the PDZ domain function synergistically in binding to inositol phospholipids.

PubMed: 16252003
DOI: 10.1038/sj.emboj.7600858

実験手法

SOLUTION NMR