IPR001331
Guanine-nucleotide dissociation stimulator, CDC24, conserved site
InterPro entry
Short name | GDS_CDC24_CS |
Description
Ras proteins are membrane-associated molecular switches that bind GTP and GDP and slowly hydrolyze GTP to GDP
[1]. 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
[2, 3]. 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. One of these families is currently known to group the CDC24 family of proteins.
References
1.The GTPase superfamily: conserved structure and molecular mechanism. Bourne HR, Sanders DA, McCormick F. Nature 349, 117-27, (1991). View articlePMID: 1898771
2.Proteins regulating Ras and its relatives. Boguski MS, McCormick F. Nature 366, 643-54, (1993). View articlePMID: 8259209
3.Ras regulation: putting back the GTP. Downward J. Curr. Biol. 2, 329-31, (1992). View articlePMID: 15335949
GO terms
biological process
molecular function
cellular component
- None
Cross References
Contributing Member Database Entry
- PROSITE patterns:PS00741