1SGH

Moesin FERM domain bound to EBP50 C-terminal peptide

1SGH の概要

• エントリーDOI: 10.2210/pdb1sgh/pdb
• 分子名称: Moesin, Ezrin-radixin-moesin binding phosphoprotein 50 (2 entities in total)
• 機能のキーワード: ferm-peptide complex, structural protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cell membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): P26038; Cytoplasm (By similarity): O14745
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 39558.65

構造登録者

Finnerty, C.M.,Chambers, D.,Ingraffea, J.,Faber, H.R.,Karplus, P.A.,Bretscher, A. (登録日: 2004-02-23, 公開日: 2004-06-29, 最終更新日: 2023-08-23)

主引用文献

Finnerty, C.M.,Chambers, D.,Ingraffea, J.,Faber, H.R.,Karplus, P.A.,Bretscher, A.
The EBP50-moesin interaction involves a binding site regulated by direct masking on the FERM domain
J.Cell.Sci., 117:1547-1552, 2004

PubMed Abstract: Members of the ezrin-radixin-moesin (ERM) protein family serve as regulated microfilament-membrane crosslinking proteins that, upon activation, bind the scaffolding protein ERM-phosphoprotein of 50 kDa (EBP50). Here we report a 3.5 A resolution diffraction analysis of a complex between the active moesin N-terminal FERM domain and a 38 residue peptide from the C terminus of EBP50. This crystallographic result, combined with sequence and structural comparisons, suggests that the C-terminal 11 residues of EBP50 binds as an alpha-helix at the same site occupied in the dormant monomer by the last 11 residues of the inhibitory moesin C-terminal tail. Biochemical support for this interpretation derives from in vitro studies showing that appropriate mutations in both the EBP50 tail peptide and the FERM domain reduce binding, and that a peptide representing just the C-terminal 14 residues of EBP50 also binds to moesin. Combined with the recent identification of the I-CAM-2 binding site on the ERM FERM domain (Hamada, K., Shimizu, T., Yonemura, S., Tsukita, S., and Hakoshima, T. (2003) EMBO J. 22, 502-514), this study reveals that the FERM domain contains two distinct binding sites for membrane-associated proteins. The contribution of each ligand to ERM function can now be dissected by making structure-based mutations that specifically affect the binding of each ligand.

PubMed: 15020681
DOI: 10.1242/jcs.01038

実験手法

X-RAY DIFFRACTION (3.5 Å)