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2VGL

AP2 CLATHRIN ADAPTOR CORE

1GW5」から置き換えられました
2VGL の概要
エントリーDOI10.2210/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: 12086608
DOI: 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)
構造検証レポート
Validation report summary of 2vgl
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-06-04に公開中

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