RasGEF domain

RasGEF domain is domain found in the CDC25 family of guanine nucleotide exchange factors for Ras-like small GTPases.

Main article: Ras (protein)
RasGEF domain
Structure of human H-Ras.[1]
Identifiers
SymbolRasGEF
PfamPF00617
InterProIPR001895
SMARTRasGEF
PROSITEPDOC00594
SCOP21bkd / SCOPe / SUPFAM
OPM protein1xd4
CDDcd00155
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1xd2C:777-963 1bkdS:777-963 1xdvB:777-963

1nvwS:777-963 1xd4A:777-963 1nvuS:777-963

1nvvS:777-963 1nvxS:777-963

Ras proteins are membrane-associated molecular switches that bind GTP and GDP and slowly hydrolyze GTP to GDP.[2] The balance between the GTP bound (active) and GDP bound (inactive) states is regulated by the opposite action of proteins activating the GTPase activity and that of proteins which promote the loss of bound GDP and the uptake of fresh GTP.[3][4] The latter proteins are known as guanine-nucleotide dissociation stimulators (GDSs) (or also as guanine-nucleotide releasing (or exchange) factors (GRFs)). Proteins that act as GDS can be classified into at least two families, on the basis of sequence similarities, the CDC24 family (see InterPro: IPR001331) and this CDC25 (RasGEF) family.

The size of the proteins of the CDC25 family range from 309 residues (LTE1) to 1596 residues (sos). The sequence similarity shared by all these proteins is limited to a region of about 250 amino acids generally located in their C-terminal section (currently the only exceptions are sos and ralGDS where this domain makes up the central part of the protein). This domain has been shown, in CDC25 an SCD25, to be essential for the activity of these proteins.

Human proteins containing this domain

KNDC1; PLCE1; RALGDS; RALGPS1; RALGPS2; RAPGEF1; RAPGEF2; RAPGEF3; RAPGEF4; RAPGEF5; RAPGEF6; RAPGEFL1; RASGEF1A; RASGEF1B; RASGEF1C; RASGRF1; RASGRF2; RASGRP1; RASGRP2; RASGRP3; RASGRP4; RGL1; RGL2; RGL3; RGL4/RGR; SOS1; SOS2;

References
  1. Boriack-Sjodin PA, Margarit SM, Bar-Sagi D, Kuriyan J (July 1998). "The structural basis of the activation of Ras by Sos". Nature. 394 (6691): 337–43. Bibcode:1998Natur.394..337B. doi:10.1038/28548. PMID 9690470. S2CID 204998911.
  2. McCormick F, Bourne HR, Sanders DA (1991). "The GTPase superfamily: conserved structure and molecular mechanism". Nature. 349 (6305): 117–127. Bibcode:1991Natur.349..117B. doi:10.1038/349117a0. PMID 1898771. S2CID 4349901.
  3. McCormick F, Boguski MS (1993). "Proteins regulating Ras and its relatives". Nature. 366 (6456): 643–654. Bibcode:1993Natur.366..643B. doi:10.1038/366643a0. PMID 8259209. S2CID 4338237.
  4. Downward J (1992). "Ras regulation: putting back the GTP". Curr. Biol. 2 (6): 329–331. doi:10.1016/0960-9822(92)90897-J. PMID 15335949. S2CID 21826028.

Further reading
This article incorporates text from the public domain Pfam and InterPro: IPR001895


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