1H0A

Epsin ENTH bound to Ins(1,4,5)P3

1H0A の概要

• エントリーDOI: 10.2210/pdb1h0a/pdb
• 関連するPDBエントリー: 1EDU 1EYH
• 分子名称: EPSIN, 1,4-DIETHYLENE DIOXIDE, D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: endocytosis, epsin, enth, clathrin, triskelion, coated vesicles, alpha-alpha superhelix, ins(1, 4, 5)p3
• 由来する生物種: RATTUS NORVEGICUS (RAT)
• 細胞内の位置: Cytoplasm: O88339
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19276.63

構造登録者

Ford, M.G.J.,McMahon, H.T.,Evans, P.R. (登録日: 2002-06-12, 公開日: 2002-10-03, 最終更新日: 2023-12-13)

主引用文献

Ford, M.G.J.,Mills, I.,Peter, B.,Vallis, Y.,Praefcke, G.,Evans, P.R.,Mcmahon, H.T.
Curvature of Clathrin-Coated Pits Driven by Epsin
Nature, 419:361-, 2002

PubMed Abstract: Clathrin-mediated endocytosis involves cargo selection and membrane budding into vesicles with the aid of a protein coat. Formation of invaginated pits on the plasma membrane and subsequent budding of vesicles is an energetically demanding process that involves the cooperation of clathrin with many different proteins. Here we investigate the role of the brain-enriched protein epsin 1 in this process. Epsin is targeted to areas of endocytosis by binding the membrane lipid phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P(2)). We show here that epsin 1 directly modifies membrane curvature on binding to PtdIns(4,5)P(2) in conjunction with clathrin polymerization. We have discovered that formation of an amphipathic alpha-helix in epsin is coupled to PtdIns(4,5)P(2) binding. Mutation of residues on the hydrophobic region of this helix abolishes the ability to curve membranes. We propose that this helix is inserted into one leaflet of the lipid bilayer, inducing curvature. On lipid monolayers epsin alone is sufficient to facilitate the formation of clathrin-coated invaginations.

PubMed: 12353027
DOI: 10.1038/NATURE01020

実験手法

X-RAY DIFFRACTION (1.7 Å)