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Three Discrete Regions of Mammalian Adenylyl Cyclase Form a Site for G sα Activation *

Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 272, Issue: 30, Page: 18849-18854
1997
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Article Description

The interaction between the α subunit of G protein G s (G sα ) and the two cytoplasmic domains of adenylyl cyclase (C 1 and C 2 ) is a key step in the stimulation of cAMP synthesis by hormones. Mutational analysis reveals that three discrete regions in the primary sequence of adenylyl cyclase affect the EC 50 values for G sα activation and thus are the affinity determinants of G sα. Based on the three-dimensional structure of C 2 ·forskolin dimer, these three regions (C 2 α2, C 2 α3/β4, and C 1 β1) are close together and form a negatively charged and hydrophobic groove the width of an α helix that can accommodate the positively charged adenylyl cyclase binding region of G sα. Two mutations in the C 2 α3/β4 region decrease the V max values of G sα activation without an increase in the EC 50 values. Since these three regions are distal to the catalytic site, the likely mechanism for G sα activation is to modulate the structure of the active site by controlling the orientation of the C 2 α2 and α3/β4 structures.

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