1OM9

Structure of the GGA1-appendage in complex with the p56 binding peptide

1OM9 の概要

• エントリーDOI: 10.2210/pdb1om9/pdb
• 関連するPDBエントリー: 1GYU 1IU1 1NA8
• 分子名称: ADP-ribosylation factor binding protein GGA1, 15-mer peptide fragment of p56 (3 entities in total)
• 機能のキーワード: beta sandwich, beta augmentation, gga, adaptin, clathrin adaptor, protein transport, signaling protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein: Q9UJY5
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 37947.37

構造登録者

Collins, B.M.,Praefcke, G.J.K.,Robinson, M.S.,Owen, D.J. (登録日: 2003-02-25, 公開日: 2003-07-29, 最終更新日: 2023-08-16)

主引用文献

Collins, B.M.,Praefcke, G.J.K.,Robinson, M.S.,Owen, D.J.
Structural basis for binding of accessory proteins by the appendage domain of GGAs
Nat.Struct.Biol., 10:607-613, 2003

PubMed Abstract: The Golgi-associated, gamma-adaptin-related, ADP-ribosylation-factor binding proteins (GGAs) and adaptor protein (AP)-1 are adaptors involved in clathrin-mediated transport between the trans-Golgi network and endosomal system. The appendage domains of GGAs and the AP-1 gamma-adaptin subunit are structurally homologous and have been proposed to bind to accessory proteins via interaction with short sequences containing phenylalanines and acidic residues. Here we present the structure of the human GGA1 appendage in complex with its cognate binding peptide from the p56 accessory protein (DDDDFGGFEAAETFD) as determined by X-ray crystallography. The interaction is governed predominantly by packing of the first two phenylalanine residues of the peptide with conserved basic and hydrophobic residues from GGA1. Additionally, several main chain hydrogen bonds cause the peptide to form an additional beta-strand on the edge of the preexisting beta-sheet of the protein. Isothermal titration calorimetry was used to assess the affinities of different peptides for the GGA and gamma-appendage domains.

PubMed: 12858163
DOI: 10.1038/nsb955

実験手法

X-RAY DIFFRACTION (2.5 Å)