Intrasteric regulation of protein kinases and phosphatases

Bruce E. Kemp, Richard B. Pearson

Research output: Contribution to journalShort SurveyOtherpeer-review

118 Citations (Scopus)

Abstract

Protein kinases and protein phosphatases are the pre-eminent regulators of cellular processes. Many of these enzymes are present in latent forms that are activated by various modulators. The inhibited form is maintained by autoinhibitory domains either within these proteins or in some instances by separate inhibitory subunits. A number of these autoinhibitory structures have been identified because of structural similarity to their enzyme's substrate. These findings indicate that the enzyme's active site may recognize either substrates or pseudosubstrate autoinhibitory. structures that turn them off. Because this form of regulation is directed at the active site it is termed intrasteric control.

Original languageEnglish
Pages (from-to)67-76
Number of pages10
JournalBBA - Molecular Cell Research
Volume1094
Issue number1
DOIs
Publication statusPublished - 13 Aug 1991
Externally publishedYes

Keywords

  • Inhibitory site
  • Intrasteric control
  • Latent form
  • Phosphatase
  • Protein kinase

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