The interactions of adenylate cyclases with P-site inhibitors

Carmen W. Dessauer; John J.G. Tesmer; Stephen R. Sprang; Alfred G. Gilman

doi:10.1016/S0165-6147(99)01310-3

The interactions of adenylate cyclases with P-site inhibitors

Carmen W. Dessauer
, John J.G. Tesmer
, Stephen R. Sprang
, Alfred G. Gilman

Division of Biological and Biomedical Sciences

Research output: Contribution to journal › Review article › peer-review

85 Scopus citations

Abstract

Recent kinetic, binding and crystallographic studies using P-site inhibitors of mammalian adenylate cyclases provide new insights into the catalytic mechanism of these highly regulated enzymes. Here, Carmen Dessauer and colleagues discuss the conformational states of adenylate cyclase, the structural determinants of inhibitor binding and the potential uses of these inhibitors as pharmacological agents.

Original language	English
Pages (from-to)	205-210
Number of pages	6
Journal	Trends in Pharmacological Sciences
Volume	20
Issue number	5
DOIs	https://doi.org/10.1016/S0165-6147(99)01310-3
State	Published - May 1 1999

Funding

Work from the authors' laboratories was supported by NIH grants DK46371 and GM34497, Welch Foundation Grants I-1229 and I-1271 and the Raymond and Ellen Willie Distinguished Chair in Molecular Neuropharmacology.

Funder number
DK46371
R37GM034497
I-1271, I-1229

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10.1016/S0165-6147(99)01310-3

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title = "The interactions of adenylate cyclases with P-site inhibitors",

abstract = "Recent kinetic, binding and crystallographic studies using P-site inhibitors of mammalian adenylate cyclases provide new insights into the catalytic mechanism of these highly regulated enzymes. Here, Carmen Dessauer and colleagues discuss the conformational states of adenylate cyclase, the structural determinants of inhibitor binding and the potential uses of these inhibitors as pharmacological agents.",

author = "Dessauer, \{Carmen W.\} and Tesmer, \{John J.G.\} and Sprang, \{Stephen R.\} and Gilman, \{Alfred G.\}",

note = "Funding Information: Work from the authors' laboratories was supported by NIH grants DK46371 and GM34497, Welch Foundation Grants I-1229 and I-1271 and the Raymond and Ellen Willie Distinguished Chair in Molecular Neuropharmacology.",

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AU - Tesmer, John J.G.

AU - Sprang, Stephen R.

AU - Gilman, Alfred G.

N1 - Funding Information: Work from the authors' laboratories was supported by NIH grants DK46371 and GM34497, Welch Foundation Grants I-1229 and I-1271 and the Raymond and Ellen Willie Distinguished Chair in Molecular Neuropharmacology.

PY - 1999/5/1

Y1 - 1999/5/1

N2 - Recent kinetic, binding and crystallographic studies using P-site inhibitors of mammalian adenylate cyclases provide new insights into the catalytic mechanism of these highly regulated enzymes. Here, Carmen Dessauer and colleagues discuss the conformational states of adenylate cyclase, the structural determinants of inhibitor binding and the potential uses of these inhibitors as pharmacological agents.

AB - Recent kinetic, binding and crystallographic studies using P-site inhibitors of mammalian adenylate cyclases provide new insights into the catalytic mechanism of these highly regulated enzymes. Here, Carmen Dessauer and colleagues discuss the conformational states of adenylate cyclase, the structural determinants of inhibitor binding and the potential uses of these inhibitors as pharmacological agents.

UR - https://www.scopus.com/pages/publications/0033136873

U2 - 10.1016/S0165-6147(99)01310-3

DO - 10.1016/S0165-6147(99)01310-3

M3 - Review article

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AN - SCOPUS:0033136873

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EP - 210

JO - Trends in Pharmacological Sciences

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ER -

The interactions of adenylate cyclases with P-site inhibitors

Abstract

Funding

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