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Science 30 June 1989: Vol. 244. no. 4912, pp. 1558 - 1564 DOI: 10.1126/science.2472670
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Articles
Science, Vol 244, Issue 4912, 1558-1564
Copyright © 1989 by American Association for the Advancement of Science
Adenylyl cyclase amino acid sequence: possible channel- or transporter-like structure
J Krupinski,
F Coussen,
HA Bakalyar,
WJ Tang,
PG Feinstein,
K Orth,
C Slaughter,
RR Reed,
and
AG Gilman
Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas 75235.
Complementary DNA's that encode an adenylyl cyclase were isolated from a bovine brain library. Most of the deduced amino acid sequence of 1134 residues is divisible into two alternating sets of hydrophobic and hydrophilic domains. Each of the two large hydrophobic domains appears to contain six transmembrane spans. Each of the two large hydrophilic domains contains a sequence that is homologous to a single cytoplasmic domain of several guanylyl cyclases; these sequences may represent nucleotide binding sites. An unexpected topographical resemblance between adenylyl cyclase and various plasma membrane channels and transporters was observed. This structural complexity suggests possible, unappreciated functions for this important enzyme.
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