Solution structure of the Ras‐binding domain of RGL

FEBS Letters

Shirouzu, Mikako²  Kigawa, Takanori²  Yokoyama, Shigeyuki²  Endo, Makoto²  Ito, Yutaka³  Kikuchi, Akira¹ 

[1] Department of Biochemistry, Hiroshima University School of Medicine, 1-2-3 Kasumi, Minami-ku, Hiroshima, Hiroshima 734-8551, Japan;Cellular Signaling Laboratory, The Institute of Physical and Chemical Research (RIKEN), 2-1 Hirosawa, Wako, Saitama 351-0198, Japan;Laboratory of Cellular and Molecular Biology, The Institute of Physical and Chemical Research (RIKEN), 2-1 Hirosawa, Wako, Saitama 351-0198, Japan

关键词: RGL;    Ras-binding domain;    GDP dissociation stimulator;    Nuclear magnetic resonance;    Solution structure;    Signal transduction;    DTT;    dithiothreitol;    GDS;    GDP dissociation stimulator;    GMPPNP;    guanosine 5′-O-(β;    γ-imidotriphosphate);    GST;    glutathione S-transferase;    RBD;    Ras-binding domain;   

DOI  :  10.1016/S0014-5793(98)01596-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The RGL protein, a homolog of the Ral GDP dissociation stimulator (RalGDS), has been identified as a downstream effector of Ras. In the present study, the solution structure of the Ras-binding domain of RGL (RGL-RBD) was determined by NMR spectroscopy. The overall fold of RGL-RBD consists of a five-stranded β-sheet and two α-helices, which is the same topology as that of RalGDS-RBD. The backbone chemical shift perturbation of RGL-RBD upon interaction with the GTP analog-bound Ras was also examined. The solution structure of RGL-RBD, especially around some of the Ras-interacting residues, is appreciably different from that of RalGDS-RBD.

【 授权许可】

Unknown