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1KY7

THE AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH AMPHIPHYSIN FXDXF

1KY7 の概要
エントリーDOI10.2210/pdb1ky7/pdb
関連するPDBエントリー1KY6 1KY7 1KYD 1KYF 1QTP 1QTS
分子名称ALPHA-ADAPTIN C, AMPHIPHYSIN (3 entities in total)
機能のキーワードprotein-peptide complex, endocytosis, endocytosis-exocytosis complex, endocytosis/exocytosis
由来する生物種Mus musculus (house mouse)
詳細
細胞内の位置Cell membrane: P17427
Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Peripheral membrane protein; Cytoplasmic side: P49418
タンパク質・核酸の鎖数2
化学式量合計29058.95
構造登録者
Brett, T.J.,Traub, L.M.,Fremont, D.H. (登録日: 2002-02-03, 公開日: 2002-06-12, 最終更新日: 2023-08-16)
主引用文献Brett, T.J.,Traub, L.M.,Fremont, D.H.
Accessory protein recruitment motifs in clathrin-mediated endocytosis.
Structure, 10:797-809, 2002
Cited by
PubMed Abstract: Clathrin-mediated endocytosis depends upon the interaction of accessory proteins with the alpha-ear of the AP-2 adaptor. We present structural characterization of these regulatory interactions. DPF and DPW motif peptides derived from eps15 and epsin bind in type I beta turn conformations to a conserved pocket on the alpha-ear platform. We show evidence for a second binding site that is DPW motif specific. The structure of a complex with an AP-2 binding segment from amphiphysin reveals a novel binding motif that we term FxDxF, which is engaged in an extended conformation by a unique surface of the platform domain. The FxDxF motif is also used by AP180 and the 170 kDa isoform of synaptojanin and can be found in several potential endocytic proteins, including HIP1, CD2AP, and PLAP. A mechanism of clathrin assembly regulation is suggested by three different AP-2 engagement modes.
PubMed: 12057195
DOI: 10.1016/S0969-2126(02)00784-0
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.15 Å)
構造検証レポート
Validation report summary of 1ky7
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2024-12-18に公開中

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