Ras-like guanine nucleotide exchange factor, N-terminal (IPR000651)

Short name: Ras-like_Gua-exchang_fac_N

Domain relationships



The crystal structure of the guanine nucleotide exchange factor (GEF) region of human Sos1 complexes with Ras has been solved [PMID: 9690470]. The structure consists of two distinct alpha helical structural domains: the N-terminal domain which seems to have a purely structural role and the C-terminal domain which is sufficient for catalytic activity and contains all residues that interact with Ras. A main feature of the catalytic domain is the protrusion of a helical hairpin important for the nucleotide-exchange mechanism. The N-terminal domain is likely to be important for the stability and correct placement of the hairpin structure.

This entry represents a domain found in several GEF for Ras-like small GTPases which lies N-terminal to the RasGef (Cdc25-like) domain.

GO terms

Biological Process

GO:0051056 regulation of small GTPase mediated signal transduction

Molecular Function

GO:0005085 guanyl-nucleotide exchange factor activity

Cellular Component

GO:0005622 intracellular

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles