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Reaction of GeF 4 with fluoride sources produces GeF 5 − anions with octahedral coordination around Ge atom due to polymerization. [6] The structural characterization of a discrete trigonal bipyramidal GeF 5 − anion was achieved by a "naked" fluoride reagent 1,3-bis(2,6-diisopropylphenyl)imidazolium fluoride.
GDP remains bound to the inactive GTPase until a GEF binds and stimulates its release. [3] The localization of GEFs can determine where in the cell a particular GTPase will be active. For example, the Ran GEF, RCC1, is present in the nucleus while the Ran GAP is present in the cytosol, modulating nuclear import and export of proteins. [8]
The inactive form of GTPases (GDP-form) are activated by a class of proteins called Guanosine nucleotide exchange factors (GEFs). GEFs catalyse nucleotide exchange by encouraging the release of GDP from the small GTPase (by displacement of the small GTPase-associated Mg 2+ ion) and GDP's replacement by GTP (which is in at least a 10-fold excess within the cell) .
Rap guanine nucleotide exchange factor (GEF) 4 (RAPGEF4), also known as exchange protein directly activated by cAMP 2 (EPAC2) is a protein that in humans is encoded by the RAPGEF4 gene. [5] [6] [7] Epac2 is a target of cAMP, a major second messenger in various cells.
eEF-1A (α) [2] mediates the entry of the aminoacyl tRNA into a free site of the ribosome. [4] EF-Ts: eEF-1B (β γ) [2] serves as the guanine nucleotide exchange factor for EF-Tu, catalyzing the release of GDP from EF-Tu. [2] EF-G: eEF-2: catalyzes the translocation of the tRNA and mRNA down the ribosome at the end of each round of polypeptide ...
RhoGEF domain describes two distinct structural domains with guanine nucleotide exchange factor (GEF) activity to regulate small GTPases in the Rho family.Rho small GTPases are inactive when bound to GDP but active when bound to GTP; RhoGEF domains in proteins are able to promote GDP release and GTP binding to activate specific Rho family members, including RhoA, Rac1 and Cdc42.
SOS1 is a guanine nucleotide exchange factor (GEF) which interacts with Ras proteins to phosphorylate GDP into GTP, or from an inactive state to an active state to signal cell proliferation. RAS genes (e.g., MIM 190020) encode membrane-bound guanine nucleotide-binding proteins that function in the transduction of signals that control cell ...
[4] RGS domains in the G protein-coupled receptor kinases are able to bind to Gq family α-subunits, but do not accelerate their GTP hydrolysis. Instead, GRKs appear to reduce Gq signaling by sequestering the active α-subunits away from effectors such as phospholipase C-β.