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Crystal structure of GGA2 VHS domain and its implication in plasticity in the ligand binding pocket
Author(s) -
Zhu Guangyu,
He Xiangyuan,
Zhai Peng,
Terzyan Simon,
Tang Jordan,
Zhang Xuejun C.
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00095-4
Subject(s) - ligand (biochemistry) , biophysics , chemistry , conformational change , crystallography , plasma protein binding , stereochemistry , biochemistry , receptor , biology
Golgi‐localized, γ‐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 Å 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.