1hg2

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[[Image:1hg2.jpg|left|200px]]
[[Image:1hg2.jpg|left|200px]]
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{{Structure
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|PDB= 1hg2 |SIZE=350|CAPTION= <scene name='initialview01'>1hg2</scene>, resolution 2.0&Aring;
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The line below this paragraph, containing "STRUCTURE_1hg2", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=IP2:Binding+Site+For+Inositol+Bisphosphates'>IP2</scene>
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|LIGAND= <scene name='pdbligand=IP2:D-MYO-INOSITOL-4,5-BISPHOSPHATE'>IP2</scene>
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{{STRUCTURE_1hg2| PDB=1hg2 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hg2 OCA], [http://www.ebi.ac.uk/pdbsum/1hg2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hg2 RCSB]</span>
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'''CALM-N N-TERMINAL DOMAIN OF CLATHRIN ASSEMBLY LYMPHOID MYELOID LEUKAEMIA PROTEIN, INOSITOL(4,5)P2 COMPLEX'''
'''CALM-N N-TERMINAL DOMAIN OF CLATHRIN ASSEMBLY LYMPHOID MYELOID LEUKAEMIA PROTEIN, INOSITOL(4,5)P2 COMPLEX'''
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[[Category: Ford, M G.J.]]
[[Category: Ford, M G.J.]]
[[Category: Mcmahon, H T.]]
[[Category: Mcmahon, H T.]]
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[[Category: adaptor]]
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[[Category: Adaptor]]
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[[Category: endocytosis]]
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[[Category: Endocytosis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:48:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:04:22 2008''
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Revision as of 15:48, 2 May 2008

Image:1hg2.jpg

Template:STRUCTURE 1hg2

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. 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 Fri May 2 18:48:47 2008

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