1h0a

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(New page: 200px<br /> <applet load="1h0a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h0a, resolution 1.70&Aring;" /> '''EPSIN ENTH BOUND TO...)
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Revision as of 16:28, 29 October 2007

Image:1h0a.gif

1h0a, resolution 1.70Å

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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. ... [(full description)]

About this Structure

1H0A is a [Single protein] structure of sequence from [Rattus norvegicus] with DIO and I3P as [ligands]. 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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