1hg2
From Proteopedia
Line 21: | Line 21: | ||
[[Category: endocytosis]] | [[Category: endocytosis]] | ||
- | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:35:50 2007'' |
Revision as of 13:31, 30 October 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 ... [(full description)]
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
Page seeded by OCA on Tue Oct 30 15:35:50 2007