1J19

Crystal structure of the radxin FERM domain complexed with the ICAM-2 cytoplasmic peptide

1J19 の概要

• エントリーDOI: 10.2210/pdb1j19/pdb
• 関連するPDBエントリー: 1E5W 1EF1 1GC6 1GC7 1ISN
• 分子名称: radixin, 16-mer peptide from Intercellular adhesion molecule-2 (3 entities in total)
• 機能のキーワード: protein-peptide complex, cell adhesion
• 由来する生物種: Mus musculus (house mouse); 詳細
• 細胞内の位置: Cell membrane; Peripheral membrane protein; Cytoplasmic side: P26043; Membrane; Single-pass type I membrane protein: P35330
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 39305.29

構造登録者

Hamada, K.,Shimizu, T.,Yonemura, S.,Tsukita, S.,Tsukita, S.,Hakoshima, T. (登録日: 2002-12-02, 公開日: 2003-03-11, 最終更新日: 2023-10-25)

主引用文献

Hamada, K.,Shimizu, T.,Yonemura, S.,Tsukita, S.,Tsukita, S.,Hakoshima, T.
Structural basis of adhesion-molecule recognition by ERM proteins revealed by the crystal structure of the radixin-ICAM-2 complex
EMBO J., 22:502-514, 2003

PubMed Abstract: ERM (ezrin/radixin/moesin) proteins recognize the cytoplasmic domains of adhesion molecules in the formation of the membrane-associated cytoskeleton. Here we report the crystal structure of the radixin FERM (4.1 and ERM) domain complexed with the ICAM-2 cytoplasmic peptide. The non-polar region of the ICAM-2 peptide contains the RxxTYxVxxA sequence motif to form a beta-strand followed by a short 3(10)-helix. It binds the groove of the phosphotyrosine-binding (PTB)-like subdomain C mediated by a beta-beta association and several side-chain interactions. The binding mode of the ICAM-2 peptide to the FERM domain is distinct from that of the NPxY motif-containing peptide binding to the canonical PTB domain. Mutation analyses based on the crystal structure reveal the determinant elements of recognition and provide the first insights into the physical link between adhesion molecules and ERM proteins.

PubMed: 12554651
DOI: 10.1093/emboj/cdg039

実験手法

X-RAY DIFFRACTION (2.4 Å)