1h0a

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spinqualitylabelsall models 1h0a, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

EPSIN ENTH BOUND TO INS(1,4,5)P3

Overview

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.

About this Structure

1H0A is a Single protein structure of sequence from Rattus norvegicus with DIO and I3P as ligands. Structure known Active Site: DI1. Full crystallographic information is available from OCA.

Reference

Curvature of clathrin-coated pits driven by epsin., Ford MG, Mills IG, Peter BJ, Vallis Y, Praefcke GJ, Evans PR, McMahon HT, Nature. 2002 Sep 26;419(6905):361-6. PMID:12353027

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