|PROSITE documentation PDOC50200|
Ras proteins are signal-transducing GTPases that cycle between inactive GDP-bound and active GTP-bound forms. Ras is a prolific signalling molecule interacting with a spectrum of effector molecules and acting through more than one signalling pathway. A domain of about 100 residues, termed RA for RalGDS/AF-6 or Ras-Associating, interacts with Ras and other small GTPases. It occurs in one or two copies in a variety of signalling molecules. It can be found associated with many other domains, such as PDZ (see <PDOC50106>), Dilute (DIL), GEF (see <PDOC00594>), myosin motor, IQ (see <PDOC50096>), C1 (see <PDOC00379>), C2 (see <PDOC00380>), protein kinase (see <PDOC00100>), VPS9 or sterile α motif (SAM) (see <PDOC50105>) [1,2,3].
Some proteins known to contain a RA domain are listed below:
Structurally, the RA domain of RalGDS consists of a five-stranded mixed β-sheet interrupted by a 12 residue α-helix and two additional small α-helices (see <PDB:1LXD>). The structure of the RA domain belongs to the ubiquitin α/β roll superfold and is similar to that of the RBD domain and the N-terminal third of the FERM domain (see <PDOC00566>) [4,5]. The RA domain forms a homodimer where the interdimer surface is composed of two cysteines (Cys 2 in each monomer) forming an intermolecular disulfide bond and two interacting intermolecular antiparallel β-sheets . The major interaction between Ras and RalGDS RA domain occurs between two antiparallel β-strands: β 2 of Ras and β 2 of RA. This interaction occurs both at the backbone as well as the side chain level (see <PDB:1LFD>) .
The profile we developed covers the entire RA domain.Last update:
January 2003 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Ponting C.P. Benjamin D.R.|
|Title||A novel family of Ras-binding domains.|
|Source||Trends Biochem. Sci. 21:422-425(1996).|
|2||Authors||Kido M. Shima F. Satoh T. Asato T. Kariya K. Kataoka T.|
|Title||Critical function of the Ras-associating domain as a primary Ras-binding site for regulation of Saccharomyces cerevisiae adenylyl cyclase.|
|Source||J. Biol. Chem. 277:3117-3123(2002).|
|3||Authors||Liao Y. Kariya K. Hu C.-D. Shibatohge M. Goshima M. Okada T. Watari Y. Gao X. Jin T.-G. Yamawaki-Kataoka Y. Kataoka T.|
|Source||J. Biol. Chem. 274:37815-37820(1999).|
|4||Authors||Huang L. Weng X. Hofer F. Martin G.S. Kim S.-H.|
|Title||Three-dimensional structure of the Ras-interacting domain of RalGDS.|
|Source||Nat. Struct. Biol. 4:609-615(1997).|
|5||Authors||Wojcik J. Girault J.-A. Labesse G. Chomilier J. Mornon J.-P. Callebaut I.|
|Title||Sequence analysis identifies a ras-associating (RA)-like domain in the N-termini of band 4.1/JEF domains and in the Grb7/10/14 adapter family.|
|Source||Biochem. Biophys. Res. Commun. 259:113-120(1999).|
|6||Authors||Huang L. Hofer F. Martin G.S. Kim S.-H.|
|Title||Structural basis for the interaction of Ras with RalGDS.|
|Source||Nat. Struct. Biol. 5:422-426(1998).|