Adenylyl Cyclase Amino Acid Sequence: Possible Channel- or Transporter-Like Structure

John Krupinski(The University of Texas Southwestern Medical Center), Françoise Coussen(The University of Texas Southwestern Medical Center), Heather A. Bakalyar(Howard Hughes Medical Institute), Wei‐Jen Tang(The University of Texas Southwestern Medical Center), Paul Feinstein(Howard Hughes Medical Institute), Kim Orth(Howard Hughes Medical Institute), Clive A. Slaughter(Howard Hughes Medical Institute), Randall R. Reed(The University of Texas Southwestern Medical Center), Alfred G. Gilman(The University of Texas Southwestern Medical Center)
Science
June 30, 1989
Cited by 743

Abstract

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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