1E5W

Structure of isolated FERM domain and first long helix of moesin

1E5W の概要

• エントリーDOI: 10.2210/pdb1e5w/pdb
• 関連するPDBエントリー: 1EF1
• 分子名称: MOESIN (2 entities in total)
• 機能のキーワード: membrane protein, moesin, ferm, erm
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Cell membrane ; Peripheral membrane protein ; Cytoplasmic side : P26038
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 41054.31

構造登録者

Edwards, S.D.,Keep, N.H. (登録日: 2000-08-03, 公開日: 2001-06-27, 最終更新日: 2024-05-08)

主引用文献

Edwards, S.D.,Keep, N.H.
The 2.7 A Crystal Structure of the Activated Ferm Domain of Moesin: An Analysis of Structural Changes on Activation
Biochemistry, 40:7061-, 2001

PubMed Abstract: Moesin binds to a large range of proteins through its N terminal FERM (band 4.1, ezrin, radixin, moesin) domain. In full-length moesin isolated from cells, this binding is masked by binding to the C-terminal domain of moesin (C-ERMAD). Activation takes place by phosphorylation of Thr 558 in the C-ERMAD, which releases the C-ERMAD. A recently determined crystal structure of a noncovalent complex of the FERM and C-ERMAD domains showed for the first time that the structure of the FERM domain consists of three subdomains, each of which is similar to known structures. The structure reported here also contains a unique 47-residue helix pointing away from the FERM domain at the start of the alpha domain, in agreement with secondary structure predictions. Removal of the C-ERMAD does not result in a huge rearrangement of the FERM domain, but comparison with the activated radixin structure shows a consistent set of small changes. Not surprisingly, the exposed C-ERMAD binding area interacts in crystal contacts. More interestingly, a negatively charged peptide binds to the inositol site in a crystal contact and causes a greater conformational change in the structure than inositol.

PubMed: 11401550
DOI: 10.1021/BI010419H

実験手法

X-RAY DIFFRACTION (2.7 Å)