2D11

Crystal structure of the Radixin FERM domain complexed with the NHERF-2 C-terminal tail peptide

2D11 の概要

• エントリーDOI: 10.2210/pdb2d11/pdb
• 関連するPDBエントリー: 1GC6 1GC7 1ISN 1J19 2D10
• 分子名称: Radixin, Na(+)/H(+) exchange regulatory cofactor NHE-RF2 (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; Endomembrane system; Peripheral membrane protein: Q15599
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 161766.72

構造登録者

Terawaki, S.,Maesaki, R.,Hakoshima, T. (登録日: 2005-08-11, 公開日: 2006-07-18, 最終更新日: 2024-03-13)

主引用文献

Terawaki, S.,Maesaki, R.,Hakoshima, T.
Structural basis for NHERF recognition by ERM proteins
Structure, 14:777-789, 2006

PubMed Abstract: The Na+/H+ exchanger regulatory factor (NHERF) is a key adaptor protein involved in the anchoring of ion channels and receptors to the actin cytoskeleton through binding to ERM (ezrin/radixin/moesin) proteins. NHERF binds the FERM domain of ERM proteins, although NHERF has no signature Motif-1 sequence for FERM binding found in adhesion molecules. The crystal structures of the radixin FERM domain complexed with the NHERF-1 and NHERF-2 C-terminal peptides revealed a peptide binding site of the FERM domain specific for the 13 residue motif MDWxxxxx(L/I)Fxx(L/F) (Motif-2), which is distinct from Motif-1. This Motif-2 forms an amphipathic alpha helix for hydrophobic docking to subdomain C of the FERM domain. This docking causes induced-fit conformational changes in subdomain C and affects binding to adhesion molecule peptides, while the two binding sites are not overlapped. Our studies provide structural paradigms for versatile ERM linkages between membrane proteins and the cytoskeleton.

PubMed: 16615918
DOI: 10.1016/j.str.2006.01.015

実験手法

X-RAY DIFFRACTION (2.81 Å)