1GC7

CRYSTAL STRUCTURE OF THE RADIXIN FERM DOMAIN

1GC7 の概要

• エントリーDOI: 10.2210/pdb1gc7/pdb
• 関連するPDBエントリー: 1EF1 1GC6
• 分子名称: RADIXIN (1 entity in total)
• 機能のキーワード: 3 subdomains, cytoskeleton, cell adhesion
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Cell membrane; Peripheral membrane protein; Cytoplasmic side: P26043
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35278.72

構造登録者

Hamada, K.,Shimizu, T.,Matsui, T.,Tsukita, S.,Tsukita, S.,Hakoshima, T. (登録日: 2000-07-21, 公開日: 2000-09-20, 最終更新日: 2023-12-27)

主引用文献

Hamada, K.,Shimizu, T.,Matsui, T.,Tsukita, S.,Hakoshima, T.
Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain.
EMBO J., 19:4449-4462, 2000

PubMed Abstract: Radixin is a member of the ezrin/radixin/moesin (ERM) family of proteins, which play a role in the formation of the membrane-associated cytoskeleton by linking actin filaments and adhesion proteins. This cross-linking activity is regulated by phosphoinositides such as phosphatidylinositol 4,5-bisphosphate (PIP2) in the downstream of the small G protein Rho. The X-ray crystal structures of the radixin FERM domain, which is responsible for membrane binding, and its complex with inositol-(1,4, 5)-trisphosphate (IP3) have been determined. The domain consists of three subdomains featuring a ubiquitin-like fold, a four-helix bundle and a phosphotyrosine-binding-like domain, respectively. These subdomains are organized by intimate interdomain interactions to form characteristic grooves and clefts. One such groove is negatively charged and so is thought to interact with basic juxta-membrane regions of adhesion proteins. IP3 binds a basic cleft that is distinct from those of pleckstrin homology domains and is located on a positively charged flat molecular surface, suggesting an electrostatic mechanism of plasma membrane targeting. Based on the structural changes associated with IP3 binding, a possible unmasking mechanism of ERM proteins by PIP2 is proposed.

PubMed: 10970839
DOI: 10.1093/emboj/19.17.4449

実験手法

X-RAY DIFFRACTION (2.8 Å)