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Solution structure of the Ras‐binding domain of RGL
Author(s) -
Kigawa Takanori,
Endo Makoto,
Ito Yutaka,
Shirouzu Mikako,
Kikuchi Akira,
Yokoyama Shigeyuki
Publication year - 1998
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(98)01596-8
Subject(s) - chemistry , domain (mathematical analysis) , biophysics , biology , mathematics , mathematical analysis
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.