1QTP

CRYSTAL STRUCTURE OF THE AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE

1QTP の概要

• エントリーDOI: 10.2210/pdb1qtp/pdb
• 分子名称: AP-2 CLATHRIN ADAPTOR ALPHA SUBUNIT (ALPHA-ADAPTIN C) (2 entities in total)
• 機能のキーワード: four-wavelength mad, selenomethionine, membrane protein
• 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: 28016.25

構造登録者

Traub, L.M.,Downs, M.A.,Westrich, J.L.,Fremont, D.H. (登録日: 1999-06-28, 公開日: 1999-07-12, 最終更新日: 2024-11-20)

主引用文献

Traub, L.M.,Downs, M.A.,Westrich, J.L.,Fremont, D.H.
Crystal structure of the alpha appendage of AP-2 reveals a recruitment platform for clathrin-coat assembly.
Proc.Natl.Acad.Sci.USA, 96:8907-8912, 1999

PubMed Abstract: AP-2 adaptors regulate clathrin-bud formation at the cell surface by recruiting clathrin trimers to the plasma membrane and by selecting certain membrane proteins for inclusion within the developing clathrin-coat structure. These functions are performed by discrete subunits of the adaptor heterotetramer. The carboxyl-terminal appendage of the AP-2 alpha subunit appears to regulate the translocation of several endocytic accessory proteins to the bud site. We have determined the crystal structure of the alpha appendage at 1.4-A resolution by multiwavelength anomalous diffraction phasing. It is composed of two distinct structural modules, a beta-sandwich domain and a mixed alpha-beta platform domain. Structure-based mutagenesis shows that alterations to the molecular surface of a highly conserved region on the platform domain differentially affect associations of the appendage with amphiphysin, eps15, epsin, and AP180, revealing a common protein-binding interface.

PubMed: 10430869
DOI: 10.1073/pnas.96.16.8907

実験手法

X-RAY DIFFRACTION (1.6 Å)