2vgl

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|PDB= 2vgl |SIZE=350|CAPTION= <scene name='initialview01'>2vgl</scene>, resolution 2.60&Aring;
|PDB= 2vgl |SIZE=350|CAPTION= <scene name='initialview01'>2vgl</scene>, resolution 2.60&Aring;
|SITE= <scene name='pdbsite=AC1:Ihp+Binding+Site+For+Chain+A'>AC1</scene>
|SITE= <scene name='pdbsite=AC1:Ihp+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=IHP:INOSITOL HEXAKISPHOSPHATE'>IHP</scene>
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|LIGAND= <scene name='pdbligand=IHP:INOSITOL+HEXAKISPHOSPHATE'>IHP</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=[[2iv8|2IV8]], [[2g30|2G30]], [[2iv9|2IV9]], [[1i31|1I31]], [[1bxx|1BXX]], [[1bw8|1BW8]], [[2vgl|2VGL]], [[2bp5|2BP5]], [[1gw5|1GW5]], [[1hes|1HES]], [[1e42|1E42]]
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vgl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vgl OCA], [http://www.ebi.ac.uk/pdbsum/2vgl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2vgl RCSB]</span>
}}
}}
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[[Category: Mccoy, A J.]]
[[Category: Mccoy, A J.]]
[[Category: Owen, D J.]]
[[Category: Owen, D J.]]
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[[Category: IHP]]
 
[[Category: adaptor]]
[[Category: adaptor]]
[[Category: alternative splicing]]
[[Category: alternative splicing]]
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[[Category: transport]]
[[Category: transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:46:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:12:03 2008''

Revision as of 02:12, 31 March 2008

Image:2vgl.jpg


PDB ID 2vgl

Drag the structure with the mouse to rotate
, resolution 2.60Å
Sites:
Ligands:
Related: 2IV8, 2G30, 2IV9, 1I31, 1BXX, 1BW8, 2VGL, 2BP5, 1GW5, 1HES, 1E42


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



AP2 CLATHRIN ADAPTOR CORE


Overview

AP2 is the best-characterized member of the family of heterotetrameric clathrin adaptor complexes that play pivotal roles in many vesicle trafficking pathways within the cell. AP2 functions in clathrin-mediated endocytosis, the process whereby cargo enters the endosomal system from the plasma membrane. We describe the structure of the 200 kDa AP2 "core" (alpha trunk, beta2 trunk, mu2, and sigma2) complexed with the polyphosphatidylinositol headgroup mimic inositolhexakisphosphate at 2.6 A resolution. Two potential polyphosphatidylinositide binding sites are observed, one on alpha and one on mu2. The binding site for Yxxphi endocytic motifs is buried, indicating that a conformational change, probably triggered by phosphorylation in the disordered mu2 linker, is necessary to allow Yxxphi motif binding. A model for AP2 recruitment and activation is proposed.

About this Structure

2VGL is a Protein complex structure of sequences from Homo sapiens, Mus musculus and Rattus norvegicus. This structure supersedes the now removed PDB entry 1GW5. Full crystallographic information is available from OCA.

Reference

Molecular architecture and functional model of the endocytic AP2 complex., Collins BM, McCoy AJ, Kent HM, Evans PR, Owen DJ, Cell. 2002 May 17;109(4):523-35. PMID:12086608

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