2VGL

AP2 CLATHRIN ADAPTOR CORE

Replaces:  1GW5

Summary for 2VGL

• Entry DOI: 10.2210/pdb2vgl/pdb
• Related: 1BW8 1BXX 1E42 1GW5 1HES 1I31 2BP5 2G30 2IV8 2IV9 2VGL
• Descriptor: ADAPTOR PROTEIN COMPLEX AP-2, ALPHA 2 SUBUNIT, AP-2 COMPLEX SUBUNIT BETA-1, AP-2 COMPLEX SUBUNIT MU-1, ... (6 entities in total)
• Functional Keywords: cytoplasmic vesicle, alternative splicing, endocytosis, lipid-binding, golgi apparatus, adaptor, membrane, transport, coated pit, phosphorylation, protein transport
• Biological source: RATTUS NORVEGICUS (RAT); More
• Total number of polymer chains: 4
• Total formula weight: 204034.86

Authors

Owen, D.J.,Collins, B.M.,McCoy, A.J.,Evans, P.R. (deposition date: 2007-11-14, release date: 2007-12-25, Last modification date: 2024-05-08)

Primary citation

Collins, B.M.,Mccoy, A.J.,Kent, H.M.,Evans, P.R.,Owen, D.J.
Molecular Architecture and Functional Model of the Endocytic Ap2 Complex
Cell(Cambridge,Mass.), 109:523-, 2002

PubMed Abstract: 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.

PubMed: 12086608
DOI: 10.1016/S0092-8674(02)00735-3

Experimental method

X-RAY DIFFRACTION (2.6 Å)