Comparison of the solution structures of microcystin-LR and motuporin

Nat Struct Biol. 1995 Feb;2(2):114-6. doi: 10.1038/nsb0295-114.

Abstract

A comparison of the structures of two cyanobacterial toxins yields insights into how they may inhibit protein phosphatase-1 and -2A and why microcystins but not motuporin may covalently modify their protein phosphatase targets.

Publication types

  • Comparative Study
  • Letter

MeSH terms

  • Amino Acid Sequence
  • Magnetic Resonance Spectroscopy
  • Marine Toxins
  • Microcystins
  • Models, Molecular*
  • Molecular Sequence Data
  • Peptides, Cyclic / chemistry*
  • Peptides, Cyclic / pharmacology
  • Phosphoprotein Phosphatases / antagonists & inhibitors*
  • Protein Binding
  • Protein Phosphatase 1
  • Protein Structure, Tertiary*
  • Solutions

Substances

  • Marine Toxins
  • Microcystins
  • Peptides, Cyclic
  • Solutions
  • motuporin
  • nodularin
  • microcystin LL
  • cyanoginosin-LA
  • Phosphoprotein Phosphatases
  • Protein Phosphatase 1
  • cyanoginosin LR