PROSITE documentation PDOC50898
Ras-binding domain (RBD) profile


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>) [1].

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 [2].

Some proteins known to contain a RBD domain are listed below:

  • Vertebrate Raf proto-oncogene serine/threonine-protein kinase.
  • Mammalian regulator of G-protein signalling 12 (RGS12) and 14 (RGS14).
  • Mammalian T-lymphoma invasion and metastasis inducing protein 1 (TIAM1). TIAM1 modulates the activity of Rho-like proteins and connects extracellular signals to cytoskeletal activities.
  • Mouse Sif and Tiam1-like exchange factor (STEF).
  • Drosophila LOCO-c1 and LOCO-c2, two proteins required for glial cell differentiation.
  • Drosophila Still life proteins (SIF) type 1 and 2. They regulate synaptic differentiation through the organization of actin cytoskeleton possibly by activating Rho-like GTPases.

The profile we developed covers the entire RBD domain.

Last update:

February 2003 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

RBD, PS50898; Ras-binding domain (RBD) profile  (MATRIX)


1AuthorsPonting C.P.
TitleRaf-like Ras/Rap-binding domains in RGS12- and still-life-like signalling proteins.
SourceJ. Mol. Med. 77:695-698(1999).
PubMed ID10606204

2AuthorsNassar N. Horn G. Herrmann C. Scherer A. McCormick F. Wittinghofer A.
TitleThe 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.
SourceNature 375:554-560(1995).
PubMed ID7791872

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