1LF8

Complex of GGA3-VHS Domain and CI-MPR C-terminal Phosphopeptide

1LF8 の概要

• エントリーDOI: 10.2210/pdb1lf8/pdb
• 関連するPDBエントリー: 1JPL 1JUQ 1JWF 1JWG
• 分子名称: ADP-ribosylation factor binding protein GGA3, Cation-independent mannose-6-phosphate receptor (3 entities in total)
• 機能のキーワード: vhs domain, protein-phosphopeptide complex, 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: Q9NZ52; Lysosome membrane; Single-pass type I membrane protein: P11717
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 84079.72

構造登録者

Kato, Y.,Misra, S.,Puertollano, R.,Hurley, J.H.,Bonifacino, J.S. (登録日: 2002-04-10, 公開日: 2002-06-26, 最終更新日: 2024-10-30)

主引用文献

Kato, Y.,Misra, S.,Puertollano, R.,Hurley, J.H.,Bonifacino, J.S.
Phosphoregulation of sorting signal-VHS domain interactions by a direct electrostatic mechanism.
Nat.Struct.Biol., 9:532-536, 2002

PubMed Abstract: Phosphorylation of the cytosolic tails of transmembrane receptors can regulate their intracellular trafficking. The structural basis for such regulation, however, has not been explained in most cases. The cytosolic tail of the cation-independent mannose 6-phosphate receptor contains a serine residue within an acidic-cluster dileucine signal that is important for the function of the receptor in the biosynthetic sorting of lysosomal hydrolases. We show here that phosphorylation of this Ser enhances interactions of the signal with its recognition module, the VHS domain of the GGA proteins. Crystallographic analyses demonstrate that the phosphoserine residue interacts electrostatically with two basic residues on the VHS domain of GGA3, thus providing an additional point of attachment of the acidic-cluster dileucine signal to its recognition module.

PubMed: 12032548

実験手法

X-RAY DIFFRACTION (2.3 Å)