2vgl | pdb_00002vgl

AP2 CLATHRIN ADAPTOR CORE

spinqualitylabelsall models 2vgl, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2vgl is a 4 chain structure with sequence from Homo sapiens, Mus musculus and Rattus norvegicus. This structure supersedes the now removed PDB entry 1gw5. The April 2007 RCSB PDB Molecule of the Month feature on Clathrin by Graham T. Johnson and David S. Goodsell is 10.2210/rcsb_pdb/mom_2007_4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: IHP Related: 2iv8, 2g30, 2iv9, 1i31, 1bxx, 1bw8, 2bp5, 1gw5, 1hes, 1e42 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Adaptin

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