High‐pressure NMR study of the complex of a GTPase Rap1A with its effector RalGDS

FEBS Letters

Yamada, Hiroaki²  Horn, Gudrun³  Kalbitzer, Hans Robert³  Maurer, Till³  Herrmann, Christian⁴  Inoue, Kyoko¹  Akasaka, Kazuyuki¹ 

[1] Graduate School of Science and Technology, Kobe University, 1-1 Rokkodai-cho, Kobe 657-8501, Japan;Faculty of Science, Kobe University, 1-1 Rokkodai-cho, Kobe 657-8501, Japan;Institute for Biophysics and Physical Biochemistry, University of Regensburg, 93040 Regensburg, Germany;Max-Planck-Institute for Molecular Physiology, 44227 Dortmund, Germany

关键词: High-pressure NMR;    Chemical shift;    RalGDS;    Rap1A;    Signal transduction;   

DOI  :  10.1016/S0014-5793(01)02809-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Unusually large non-linear ¹H and ¹⁵N nuclear magnetic resonance chemical shifts against pressure have been detected for individual amide groups of the Ras-binding domain of Ral guanine dissociation stimulator (GDS). The non-linear response is largest in the region of the protein remote from the Rap1A-binding site, which increases by about two-fold by the complex formation with its effector protein Rap1A. The unusual non-linearity is explained by the increasing population of another conformer (N′), lying energetically above the basic native conformer (N), at higher pressure. It is considered likely that the conformational change from N to N′ in the Ras-binding domain of RalGDS works as a switch to transmit the effector signal further to molecules of different RalGDS-dependent signaling pathways.

【 授权许可】

Unknown