Ras-associating domain
IPR000159
Definition
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, Dilute (DIL), GEF, myosin motor, IQ, C1, C2, protein kinase, VPS9 or sterile alpha motif (SAM) [[cite:PMID:8987396], [cite:PMID:11723130]]. 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. 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 [[cite:PMID:9253406], [cite:PMID:10334925]]. 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 PMID:9253406. The major interaction between Ras and RalGDS RA domain occurs between two antiparallel β-strands: β2 of Ras and β2 of RA. This interaction occurs both at the backbone as well as the side chain level PMID:9628477.
38 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
Loading the interactive Seroatlas explorer...