2G30

beta appendage of AP2 complexed with ARH peptide

2G30 の概要

• エントリーDOI: 10.2210/pdb2g30/pdb
• 分子名称: AP-2 complex subunit beta-1, 16-mer peptide from Low density lipoprotein receptor adapter protein 1, peptide sequence AAF, ... (4 entities in total)
• 機能のキーワード: alpha-helical arh peptide, platform domain, sandwich domain, endocytosis, adaptor, endocytosis-exocytosis complex, endocytosis/exocytosis
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cell membrane: P63010; Cytoplasm: Q5SW96
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 31178.66

構造登録者

Edeling, M.A.,Collins, B.M.,Traub, L.M.,Owen, D.J. (登録日: 2006-02-17, 公開日: 2006-03-14, 最終更新日: 2023-10-25)

主引用文献

Edeling, M.A.,Mishra, S.K.,Keyel, P.A.,Steinhauser, A.L.,Collins, B.M.,Roth, R.,Heuser, J.E.,Owen, D.J.,Traub, L.M.
Molecular Switches Involving the AP-2 beta2 Appendage Regulate Endocytic Cargo Selection and Clathrin Coat Assembly
Dev.Cell, 10:329-342, 2006

PubMed Abstract: Clathrin-associated sorting proteins (CLASPs) expand the repertoire of endocytic cargo sorted into clathrin-coated vesicles beyond the transmembrane proteins that bind physically to the AP-2 adaptor. LDL and GPCRs are internalized by ARH and beta-arrestin, respectively. We show that these two CLASPs bind selectively to the AP-2 beta2 appendage platform via an alpha-helical [DE](n)X(1-2)FXX[FL]XXXR motif, and that this motif also occurs and is functional in the epsins. In beta-arrestin, this motif maintains the endocytosis-incompetent state by binding back on the folded core of the protein in a beta strand conformation. Triggered via a beta-arrestin/GPCR interaction, the motif must be displaced and must undergo a strand to helix transition to enable the beta2 appendage binding that drives GPCR-beta-arrestin complexes into clathrin coats. Another interaction surface on the beta2 appendage sandwich is identified for proteins such as eps15 and clathrin, suggesting a mechanism by which clathrin displaces eps15 to lattice edges during assembly.

PubMed: 16516836
DOI: 10.1016/j.devcel.2006.01.016

実験手法

X-RAY DIFFRACTION (1.6 Å)