Not exact matches
The 673 - kilodalton protease
complex consists of 14 copies of two different
subunits,
alpha and beta, forming a barrel - shaped structure of four stacked rings.
Heterotrimeric guanine nucleotide - binding regulatory proteins (G proteins) dissociate into guanosine triphosphate (GTP)- bound
alpha subunits and a
complex of beta and gamma
subunits after interaction with receptors.
(The two
alpha subunits may bind either to the proNGF dimer before cleavage or to the
complex of the gamma
subunit and the NGF dimer after cleavage.)
In 1967 Silvio S. Varon and Eric M. Shooter of the Stanford University School of Medicine isolated NGF by a different procedure and found that the NGF dimer was present as a stable
complex with two copies each of two other proteins, which they designated the
alpha and gamma
subunits.
No one knew if this tail — also known as the C - terminus of the
alpha subunit — touches anything else in the core of the RNA polymerase
complex.