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G-proteins
Guanine Nucleotide-Binding Proteins
bind guanine nucleotides
GDP
GTP
GTP to GDP
GTP can be hydrolyzed by loss of phosphate into GDP
G-proteins have enzymatic activity that catalyze hydrolysis
GTPase activity
enzymatic activity in G-proteins that catalyze hydrolysis of GTP to GDP
G-proteins binding conditions
G-proteins must release GDP to bind to another GTP molecule
G-protein binding affinity
will bind to GTP if concentration is high enough
in cells GTP concentration usually much higher than GDP concentration, which means G-protein much more likely to bind to GTP
G-protein conformation
Active:
GTP-bound form of G-protein, has different conformation than
Inactive form:
GDP-bound form
form with no nucleotide
GAPs
GTPase Activating Protein
regulate activity of G-protein
stimulate hydrolysis of GTP into GDP by G-protein
favor inactive state
GEPs
Guanine Nucleotide Exchange Factors
stimulate release of GDP by G-protein
leads to empty G-protein, which can bind to GTP
favor active state of G-protein
G-proteins act like
molecular switches
can be on/off
can be quickly switched between on/off states
key for temporal and spatial recognition of cellular processes
G-proteins catalyze
GTP hydrolysis
GTP-bound state
active conformation
GDP-bound state
inactive conformation
GAPs
stimulate GTP hydrolysis/inactive state
GEFs
stimulate GDP release/active state