The interactions of adenylate cyclases with P-site inhibitors

被引：81

作者：

Dessauer, CW ^{[1
]}

Tesmer, JJG

Sprang, SR

Gilman, AG

机构：

[1] Univ Texas, Hlth Sci Ctr, Dept Integrat Biol Pharmacol & Physiol, Dallas, TX 75235 USA

[2] Univ Texas, SW Med Ctr, Howard Hughes Med Inst, Dept Pharmacol, Dallas, TX 75235 USA

来源：

TRENDS IN PHARMACOLOGICAL SCIENCES | 1999年 / 20卷 / 05期

关键词：

D O I：

10.1016/S0165-6147(99)01310-3

中图分类号：

R9 [药学];

学科分类号：

1007 ;

摘要：

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.

引用

页码：205 / 210

页数：6

共 47 条

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