1hg2

From Proteopedia

Revision as of 14:30, 5 November 2007

CALM-N N-TERMINAL DOMAIN OF CLATHRIN ASSEMBLY LYMPHOID MYELOID LEUKAEMIA PROTEIN, INOSITOL(4,5)P2 COMPLEX

Overview

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.

About this Structure

1HG2 is a Single protein structure of sequence from Rattus norvegicus with IP2 as ligand. Structure known Active Site: IP2. Full crystallographic information is available from OCA.

Reference

Simultaneous binding of PtdIns(4,5)P2 and clathrin by AP180 in the nucleation of clathrin lattices on membranes., Ford MG, Pearse BM, Higgins MK, Vallis Y, Owen DJ, Gibson A, Hopkins CR, Evans PR, McMahon HT, Science. 2001 Feb 9;291(5506):1051-5. PMID:11161218

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