1W80

Crystal structure of the alpha-adaptin appendage domain, from the AP2 adaptor complex, bound to 2 peptides from Synaptojanin170

1W80 の概要

• エントリーDOI: 10.2210/pdb1w80/pdb
• 関連するPDBエントリー: 1B9K 1GW5 1KY6 1KY7 1KYD 1KYF 1KYU 1QTP 1QTS
• 分子名称: ADAPTER-RELATED PROTEIN COMPLEX 2 ALPHA 2 SUBUNIT, SYNAPTOJANIN 1, BENZAMIDINE, ... (8 entities in total)
• 機能のキーワード: endocytosis/exocytosis, endocytosis, alpha-adaptin appendage, adaptor complex, ap2, synaptojanin, exocytosis, lipid-binding, endocytosis-exocytosis complex
• 由来する生物種: MUS MUSCULUS (MOUSE); 詳細
• 細胞内の位置: Cell membrane: P17427; Cytoplasm (By similarity): O43426 O43426
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 31404.42

構造登録者

Ford, M.G.J.,Praefcke, G.J.K.,McMahon, H.T. (登録日: 2004-09-14, 公開日: 2004-10-27, 最終更新日: 2023-12-13)

主引用文献

Praefcke, G.J.K.,Ford, M.G.J.,Schmid, E.M.,Olesen, L.E.,Gallop, J.L.,Peak-Chew, S.-Y.,Vallis, Y.,Babu, M.M.,Mills, I.G.,Mcmahon, H.T.
Evolving Nature of the Ap2 Alpha-Appendage Hub During Clathrin-Coated Vesicle Endocytosis.
Embo J., 23:4371-, 2004

PubMed Abstract: Clathrin-mediated endocytosis involves the assembly of a network of proteins that select cargo, modify membrane shape and drive invagination, vesicle scission and uncoating. This network is initially assembled around adaptor protein (AP) appendage domains, which are protein interaction hubs. Using crystallography, we show that FxDxF and WVxF peptide motifs from synaptojanin bind to distinct subdomains on alpha-appendages, called 'top' and 'side' sites. Appendages use both these sites to interact with their binding partners in vitro and in vivo. Occupation of both sites simultaneously results in high-affinity reversible interactions with lone appendages (e.g. eps15 and epsin1). Proteins with multiple copies of only one type of motif bind multiple appendages and so will aid adaptor clustering. These clustered alpha(appendage)-hubs have altered properties where they can sample many different binding partners, which in turn can interact with each other and indirectly with clathrin. In the final coated vesicle, most appendage binding partners are absent and thus the functional status of the appendage domain as an interaction hub is temporal and transitory giving directionality to vesicle assembly.

PubMed: 15496985
DOI: 10.1038/SJ.EMBOJ.7600445

実験手法

X-RAY DIFFRACTION (1.9 Å)