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 Slaughter; Randall R. Reed; Alfred G. Gilman

doi:10.1126/science.2472670

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 Slaughter, Randall R. Reed, Alfred G. Gilman

Research output: Contribution to journal › Article › peer-review

606 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 language	English (US)
Pages (from-to)	1558-1564
Number of pages	7
Journal	Science
Volume	244
Issue number	4912
DOIs	https://doi.org/10.1126/science.2472670
State	Published - 1989
Externally published	Yes

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title = "Adenylyl cyclase amino acid sequence: Possible channel- or transporter-like stucture",

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.",

author = "John Krupinski and Fran{\c c}oise Coussen and Bakalyar, {Heather A.} and Tang, {Wei Jen} and Feinstein, {Paul G.} and Kim Orth and Clive Slaughter and Reed, {Randall R.} and Gilman, {Alfred G.}",

year = "1989",

doi = "10.1126/science.2472670",

language = "English (US)",

volume = "244",

pages = "1558--1564",

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T1 - Adenylyl cyclase amino acid sequence

T2 - Possible channel- or transporter-like stucture

AU - Krupinski, John

AU - Coussen, Françoise

AU - Bakalyar, Heather A.

AU - Tang, Wei Jen

AU - Feinstein, Paul G.

AU - Orth, Kim

AU - Slaughter, Clive

AU - Reed, Randall R.

AU - Gilman, Alfred G.

PY - 1989

Y1 - 1989

N2 - 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.

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

Abstract

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