2VGL の概要
エントリーDOI | 10.2210/pdb2vgl/pdb |
関連するPDBエントリー | 1BW8 1BXX 1E42 1GW5 1HES 1I31 2BP5 2G30 2IV8 2IV9 2VGL |
分子名称 | ADAPTOR PROTEIN COMPLEX AP-2, ALPHA 2 SUBUNIT, AP-2 COMPLEX SUBUNIT BETA-1, AP-2 COMPLEX SUBUNIT MU-1, ... (6 entities in total) |
機能のキーワード | cytoplasmic vesicle, alternative splicing, endocytosis, lipid-binding, golgi apparatus, adaptor, membrane, transport, coated pit, phosphorylation, protein transport |
由来する生物種 | RATTUS NORVEGICUS (RAT) 詳細 |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 204034.86 |
構造登録者 | Owen, D.J.,Collins, B.M.,McCoy, A.J.,Evans, P.R. (登録日: 2007-11-14, 公開日: 2007-12-25, 最終更新日: 2024-05-08) |
主引用文献 | 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 Cited by 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: 12086608DOI: 10.1016/S0092-8674(02)00735-3 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.6 Å) |
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