1MHQ

Crystal Structure Of Human GGA2 VHS Domain

1MHQ の概要

• エントリーDOI: 10.2210/pdb1mhq/pdb
• 分子名称: ADP-ribosylation factor binding protein GGA2 (2 entities in total)
• 機能のキーワード: super helix, protein transport
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Golgi apparatus, trans-Golgi network membrane ; Peripheral membrane protein : Q9UJY4
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 34215.61

構造登録者

Zhu, G.,Zhang, X.C. (登録日: 2002-08-20, 公開日: 2003-03-11, 最終更新日: 2024-11-13)

主引用文献

Zhu, G.,He, X.,Terzyan, S.,Zhai, P.,Tang, J.,Zhang, X.C.
Crystal structure of GGA2 VHS domain and its implication in plasticity in the ligand binding pocket
FEBS LETT., 537:171-176, 2003

PubMed Abstract: Golgi-localized, gamma-ear-containing, ARF binding (GGA) proteins regulate intracellular vesicle transport by recognizing sorting signals on the cargo surface in the initial step of the budding process. The VHS (VPS27, Hrs, and STAM) domain of GGA binds with the signal peptides. Here, a crystal structure of the VHS domain of GGA2 is reported at 2.2 A resolution, which permits a direct comparison with that of homologous proteins, GGA1 and GGA3. Significant structural difference is present in the loop between helices 6 and 7, which forms part of the ligand binding pocket. Intrinsic fluorescence spectroscopic study indicates that this loop undergoes a conformational change upon ligand binding. Thus, the current structure suggests that a conformational change induced by ligand binding occurs in this part of the ligand pocket.

PubMed: 12606052
DOI: 10.1016/S0014-5793(03)00095-4

実験手法

X-RAY DIFFRACTION (2.2 Å)