1KY7
THE AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH AMPHIPHYSIN FXDXF
1KY7 の概要
エントリーDOI | 10.2210/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 | |
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: 12057195DOI: 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) |
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