Hr. Bourne, GTPASES - A FAMILY OF MOLECULAR SWITCHES AND CLOCKS, Philosophical transactions-Royal Society of London. Biological sciences, 349(1329), 1995, pp. 283-289
Members of the GTPase superfamily share a core domain with a conserved
three-dimensional structure and a common GTPase cycle, but perform a
wide variety of regulatory tasks in eukaryotic cells. Evolution has cr
eated functional diversity from the conserved GTPase structure in two
principal ways: (i) by combining in the product of a single gene the c
ore GTPase domain attached to one or more additional folded domains; (
ii) by building around a core GTPase an assembly of proteins encoded b
y different genes. Analysis of the patterns of conserved amino acid si
de chains on surfaces of Ga proteins reveals interfaces with other pro
teins in the G-protein signal linking device.