1hfa: Difference between revisions

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.

1HFA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with PIO as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: PIO. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HFA OCA].  

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