2JKT

AP2 CLATHRIN ADAPTOR CORE with CD4 Dileucine peptide RM(phosphoS) EIKRLLSE Q to E mutant

2JKT の概要

• エントリーDOI: 10.2210/pdb2jkt/pdb
• 関連するPDBエントリー: 2JKR
• 分子名称: AP-2 COMPLEX SUBUNIT ALPHA-2, AP-2 COMPLEX SUBUNIT BETA-1, AP-2 COMPLEX SUBUNIT SIGMA-1, ... (7 entities in total)
• 機能のキーワード: alternative splicing, phosphoprotein, phosphorylation, protein transport, adaptor, membrane, transport, coated pit, endocytosis, cell membrane, lipid-binding
• 由来する生物種: MUS MUSCULUS (MOUSE); 詳細
• 細胞内の位置: Cell membrane: P63010 P62743; Cell membrane (By similarity): P84092
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 412877.04

構造登録者

Owen, D.J.,McCoy, A.J.,Kelly, B.T.,Evans, P.R. (登録日: 2008-08-29, 公開日: 2008-10-28, 最終更新日: 2024-11-13)

主引用文献

Kelly, B.T.,Mccoy, A.J.,Spaete, K.,Miller, S.E.,Evans, P.R.,Hoening, S.,Owen, D.J.
A Structural Explanation for the Binding of Endocytic Dileucine Motifs by the Ap2 Complex.
Nature, 456:976-, 2008

PubMed Abstract: Most transmembrane proteins are selected as transport vesicle cargo through the recognition of short, linear amino acid motifs in their cytoplasmic portions by vesicle coat proteins. In the case of clathrin-coated vesicles (CCVs) the motifs are recognised by clathrin adaptors. The AP2 adaptor complex (subunits α,β2,μ2,σ2) recognises both major endocytic motifs: YxxΦ motifs and [DE]xxxL[LI] acidic dileucine motifs. Here we describe the binding of AP2 to the endocytic dileucine motif from CD4 . The major recognition events are the two leucine residues binding in hydrophobic pockets on σ2. The hydrophilic residue four residues upstream from the first leucine sits on a positively charged patch made from residues on σ2 and α subunits. Mutations in key residues inhibit the binding of AP2 to ‘acidic dileucine’ motifs displayed in liposomes containing PtdIns4,5P, but do not affect binding to YxxΦ motifs via μ2. In the ‘inactive’ AP2 core structure , both motif binding sites are blocked by different parts of the β2 subunit. To allow a dileucine motif to bind, the β2 N-terminus is displaced and becomes disordered; however, in this structure the YxxΦ binding site on μ2 remains blocked.

PubMed: 19140243
DOI: 10.1038/NATURE07422

実験手法

X-RAY DIFFRACTION (3.4 Å)