NMR structures of phospholipase A2 reveal conformational changes during interfacial activation

Bert Van Den Berg, Marco Tessari, Rolf Boelens, Ruud Dijkman, Gerard H. De Haas, Robert Kaptein, Hubertus M. Verheij

Research output: Contribution to journalArticleAcademicpeer-review

Abstract

It has long been proposed that the higher activity of phospholipase A2 (PLA2) for substrates presented as multimolecular aggregates compared to dispersed molecules (interfacial activation) arises due to a conformational change in the enzyme. X-ray studies have, however, failed to identify any such change. Here we report the solution structures of porcine pancreatic PLA2 both free and as a ternary complex with micelles and a competitive inhibitor. Important differences between these structures indicate that conformational changes may play an important role in the mechanism of interfacial activation in PLA2s.
Original languageEnglish
Pages (from-to)402-406
Number of pages5
JournalNature Structural Biology
Volume2
Issue number5
DOIs
Publication statusPublished - 1 May 1995

Keywords

  • phospholipase A2
  • article
  • competitive inhibition
  • conformational transition
  • enzyme activation
  • enzyme activity
  • enzyme conformation
  • nonhuman
  • nuclear magnetic resonance
  • priority journal
  • structure analysis
  • pig

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