1B9K

ALPHA-ADAPTIN APPENDAGE DOMAIN, FROM CLATHRIN ADAPTOR AP2

1B9K の概要

• エントリーDOI: 10.2210/pdb1b9k/pdb
• 分子名称: PROTEIN (ALPHA-ADAPTIN APPENDAGE DOMAIN) (2 entities in total)
• 機能のキーワード: endocytosis, adaptor, endocytosis-exocytosis complex, endocytosis/exocytosis
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Cell membrane: P17427
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27016.77

構造登録者

Owen, D.J.,Evans, P.R. (登録日: 1999-02-11, 公開日: 1999-07-06, 最終更新日: 2023-12-27)

主引用文献

Owen, D.J.,Vallis, Y.,Noble, M.E.,Hunter, J.B.,Dafforn, T.R.,Evans, P.R.,McMahon, H.T.
A structural explanation for the binding of multiple ligands by the alpha-adaptin appendage domain.
Cell(Cambridge,Mass.), 97:805-815, 1999

PubMed Abstract: The alpha subunit of the endocytotic AP2 adaptor complex contains a 30 kDa "appendage" domain, which is joined to the rest of the protein via a flexible linker. The 1.9 A resolution crystal structure of this domain reveals a single binding site for its ligands, which include amphiphysin, Eps15, and epsin. This domain when overexpressed in COS7 fibroblasts is shown to inhibit transferrin uptake, whereas mutants in which interactions with its binding partners are abolished do not. DPF/W motifs present in appendage domain-binding partners are shown to play a crucial role in their interactions with the domain. A single site for binding multiple ligands would allow for temporal and spatial regulation in the recruitment of components of the endocytic machinery.

PubMed: 10380931
DOI: 10.1016/S0092-8674(00)80791-6

実験手法

X-RAY DIFFRACTION (1.9 Å)