The interactions of adenylate cyclases with P-site inhibitors

Trends Pharmacol Sci. 1999 May;20(5):205-10. doi: 10.1016/s0165-6147(99)01310-3.


Recent kinetic, binding and crystallographic studies using P-site inhibitors of mammalian adenylate bases 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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Adenylyl Cyclase Inhibitors*
  • Adenylyl Cyclases / chemistry
  • Adenylyl Cyclases / metabolism
  • Animals
  • Catalytic Domain
  • Crystallography
  • Enzyme Inhibitors / chemistry
  • Enzyme Inhibitors / pharmacology*
  • Enzyme Inhibitors / therapeutic use
  • Models, Molecular
  • Protein Binding
  • Protein Conformation


  • Adenylyl Cyclase Inhibitors
  • Enzyme Inhibitors
  • Adenylyl Cyclases