Adenylyl cyclase amino acid sequence: Possible channel- or transporter-like stucture

John Krupinski, Françoise Coussen, Heather A. Bakalyar, Wei Jen Tang, Paul G. Feinstein, Kim Orth, Clive A. Slaughter, Randall R. Reed, Alfred G. Gilman

Research output: Contribution to journalArticle

486 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)1558-1564
Number of pages7
JournalScience
Volume244
Issue number4912
DOIs
StatePublished - Jan 1 1989
Externally publishedYes

    Fingerprint

ASJC Scopus subject areas

  • General

Cite this

Krupinski, J., Coussen, F., Bakalyar, H. A., Tang, W. J., Feinstein, P. G., Orth, K., Slaughter, C. A., Reed, R. R., & Gilman, A. G. (1989). Adenylyl cyclase amino acid sequence: Possible channel- or transporter-like stucture. Science, 244(4912), 1558-1564. https://doi.org/10.1126/science.2472670