1HG5

CALM-N N-terminal domain of clathrin assembly lymphoid myeloid leukaemia protein, inositol(1,2,3,4,5,6)P6 complex

1HG5 の概要

• エントリーDOI: 10.2210/pdb1hg5/pdb
• 関連するPDBエントリー: 1HF8 1HFA 1HG2
• 分子名称: CLATHRIN ASSEMBLY PROTEIN SHORT FORM, INOSITOL HEXAKISPHOSPHATE (3 entities in total)
• 機能のキーワード: endocytosis, adaptor
• 由来する生物種: RATTUS NORVEGICUS (NORWAY RAT)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33525.82

構造登録者

Ford, M.G.J.,Evans, P.R.,McMahon, H.T. (登録日: 2000-12-12, 公開日: 2001-02-12, 最終更新日: 2023-12-13)

主引用文献

Ford, M.G.J.,Pearse, B.M.F.,Higgins, M.K.,Vallis, Y.,Owen, D.J.,Gibson, A.,Hopkins, C.R.,Evans, P.R.,Mcmahon, H.T.
Simultaneous Binding of Ptdins(4,5)P2 and Clathrin by Ap180 in the Nucleation of Clathrin Lattices on Membranes
Science, 291:1051-, 2001

PubMed Abstract: Adaptor protein 180 (AP180) and its homolog, clathrin assembly lymphoid myeloid leukemia protein (CALM), are closely related proteins that play important roles in clathrin-mediated endocytosis. Here, we present the structure of the NH2-terminal domain of CALM bound to phosphatidylinositol-4,5- bisphosphate [PtdIns(4,5)P2] via a lysine-rich motif. This motif is found in other proteins predicted to have domains of similar structure (for example, Huntingtin interacting protein 1). The structure is in part similar to the epsin NH2-terminal (ENTH) domain, but epsin lacks the PtdIns(4,5)P2-binding site. Because AP180 could bind to PtdIns(4,5)P2 and clathrin simultaneously, it may serve to tether clathrin to the membrane. This was shown by using purified components and a budding assay on preformed lipid monolayers. In the presence of AP180, clathrin lattices formed on the monolayer. When AP2 was also present, coated pits were formed.

PubMed: 11161218
DOI: 10.1126/SCIENCE.291.5506.1051

実験手法

X-RAY DIFFRACTION (2 Å)