2D2Q

Crystal structure of the dimerized radixin FERM domain

2D2Q の概要

• エントリーDOI: 10.2210/pdb2d2q/pdb
• 関連するPDBエントリー: 1GC6 1GC7 1J19
• 分子名称: Radixin (1 entity in total)
• 機能のキーワード: homo dimer, masking, 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: 2
• 化学式量合計: 73560.86

構造登録者

Kitano, K.,Yusa, F.,Hakoshima, T. (登録日: 2005-09-15, 公開日: 2006-04-18, 最終更新日: 2024-03-13)

主引用文献

Kitano, K.,Yusa, F.,Hakoshima, T.
Structure of dimerized radixin FERM domain suggests a novel masking motif in C-terminal residues 295-304
ACTA CRYSTALLOGR.,SECT.F, 62:340-345, 2006

PubMed Abstract: ERM (ezrin/radixin/moesin) proteins bind to the cytoplasmic tail of adhesion molecules in the formation of the membrane-associated cytoskeleton. The binding site is located in the FERM (4.1 and ERM) domain, a domain that is masked in the inactive form. A conventional masking motif, strand 1 (residues 494-500 in radixin), has previously been identified in the C-terminal tail domain. Here, the crystal structure of dimerized radixin FERM domains (residues 1-310) is presented in which the binding site of one molecule is occupied by the C-terminal residues (residues 295-304, strand 2) of the other molecule. The residues contain a conserved motif that is compatible with that identified in the adhesion molecules. The residues might serve as a second masking region in the inactive form of ERM proteins.

PubMed: 16582480
DOI: 10.1107/S1744309106010062

実験手法

X-RAY DIFFRACTION (2.8 Å)