|PROSITE documentation PDOC50898 [for PROSITE entry PS50898]|
Ras and heterotrimeric G proteins' α subunits are signal-transducing GTPases that cycle between inactive GDP-bound and active GTP-bound forms. The activities of these GTPases are regulated in part by GTPase-activating protein (GAPs) that stimulate hydrolysis of GTP, and guanine nucleotide exchange factors (GEFs) that stimulate GDP release. Ras and G α GTPases are prolific signalling molecules interacting with a spectrum of effector molecules and acting through more than one signalling pathway. The Ras-binding domain (RBD) is an independent domain of about 75 residues, which is sufficient for GTP-dependent binding of Ras and other G α GTPases. The RBD domain can be present singly or in tandem and it can be found associated with many other domains, such as PDZ (see <PDOC50106>), RGS (see <PDOC50132>), PID (see <PDOC00907>), PH (see <PDOC50003>), C1 (see <PDOC00379>), DH (see <PDOC00605>), or protein kinase (see <PDOC00100>) .
Structurally, the RBD domain of Raf-1 consists of a five-stranded mixed β-sheet with an interrupted α-helix and two additional small α-helices (see <PDB:1GUA>). The structure of the RBD domain belongs to the ubiquitin α/β roll superfold and is similar to that of the RA domain (see <PDOC50200>) despite the lack of significant sequence identity. The major interaction between Ras and Raf-1 RBD domain occurs between two antiparallel β-strands: β 2 of Ras and β 2 of RBD .
Some proteins known to contain a RBD domain are listed below:
The profile we developed covers the entire RBD domain.Last update:
February 2003 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|Title||Raf-like Ras/Rap-binding domains in RGS12- and still-life-like signalling proteins.|
|Source||J. Mol. Med. 77:695-698(1999).|
|2||Authors||Nassar N. Horn G. Herrmann C. Scherer A. McCormick F. Wittinghofer A.|
|Title||The 2.2 A crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue.|