1hfa: Difference between revisions

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[[Image:1hfa.jpg|left|200px]]<br /><applet load="1hfa" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1hfa.jpg|left|200px]]
caption="1hfa, resolution 2.0&Aring;" />
 
'''CALM-N N-TERMINAL DOMAIN OF CLATHRIN ASSEMBLY LYMPHOID MYELOID LEUKAEMIA PROTEIN, PI(4,5)P2 COMPLEX'''<br />
{{Structure
|PDB= 1hfa |SIZE=350|CAPTION= <scene name='initialview01'>1hfa</scene>, resolution 2.0&Aring;
|SITE= <scene name='pdbsite=PIO:Binding+Site+For+Inositol+Bisphosphates'>PIO</scene>
|LIGAND= <scene name='pdbligand=PIO:L-ALPHA-D-MYOPHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE, D(+)SN1,2DI-O-OCTANOYLGLYCERYL'>PIO</scene>
|ACTIVITY=
|GENE=
}}
 
'''CALM-N N-TERMINAL DOMAIN OF CLATHRIN ASSEMBLY LYMPHOID MYELOID LEUKAEMIA PROTEIN, PI(4,5)P2 COMPLEX'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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 <scene name='pdbligand=PIO:'>PIO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=PIO:Binding+Site+For+Inositol+Bisphosphates'>PIO</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HFA OCA].  
1HFA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HFA OCA].  


==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11161218 11161218]
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:[http://www.ncbi.nlm.nih.gov/pubmed/11161218 11161218]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: endocytosis]]
[[Category: endocytosis]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:00:41 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:36:26 2008''

Revision as of 09:36, 20 March 2008

File:1hfa.jpg


Drag the structure with the mouse to rotate
1hfa, resolution 2.0Å
Sites: PIO
Ligands: PIO
Coordinates: save as pdb, mmCIF, xml



CALM-N N-TERMINAL DOMAIN OF CLATHRIN ASSEMBLY LYMPHOID MYELOID LEUKAEMIA PROTEIN, PI(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

1HFA 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

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