Solution structure of the Ras-binding domain of RGL.
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 beta-sheet and two alpha-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.
Kigawa
T
T
Cellular Signaling Laboratory, The Institute of Physical and Chemical Research (RIKEN), Wako, Saitama, Japan.
Endo
M
M
Ito
Y
Y
Shirouzu
M
M
Kikuchi
A
A
Yokoyama
S
S
D000595:Amino Acid Sequence; D019204:GTP-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D020662:Guanine Nucleotide Exchange Factors; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D011485:Protein Binding; D017433:Protein Structure, Secondary; D012996:Solutions; D018631:ras Proteins / Q000378:metabolism*
D020662:Guanine Nucleotide Exchange Factors; D012996:Solutions; D019204:GTP-Binding Proteins; D018631:ras Proteins