title: Solution structure of the Ras-binding domain of RGL.
abstract: 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.
authors.affiliation: Cellular Signaling Laboratory, The Institute of Physical and Chemical Research (RIKEN), Wako, Saitama, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Kigawa
authors.forename: M
authors.initials: M
authors.lastname: Endo
authors.forename: Y
authors.initials: Y
authors.lastname: Ito
authors.forename: M
authors.initials: M
authors.lastname: Shirouzu
authors.forename: A
authors.initials: A
authors.lastname: Kikuchi
authors.forename: S
authors.initials: S
authors.lastname: Yokoyama
mesh_terms: 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*
chemical_list: D020662:Guanine Nucleotide Exchange Factors; D012996:Solutions; D019204:GTP-Binding Proteins; D018631:ras Proteins