High-throughput screening of catalytically inactive mutants of protein tyrosine phosphatases (PTPs) in a phosphopeptide microarray

Chem Commun (Camb). 2009 Feb 14:(6):677-9. doi: 10.1039/b817853d. Epub 2008 Dec 12.

Abstract

We report herein a novel phosphopeptide microarray capable of noncovalently "trapping" catalytically inactive mutants of protein tyrosine phosphatases (PTPs), and its application in high-throughput determination of PTP substrate specificity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Biocatalysis*
  • Drug Design
  • Enzyme Inhibitors / pharmacology
  • Humans
  • Mutant Proteins / antagonists & inhibitors
  • Mutant Proteins / genetics*
  • Mutant Proteins / metabolism*
  • Mutation*
  • Phosphopeptides / chemistry
  • Phosphopeptides / metabolism*
  • Protein Array Analysis
  • Protein Tyrosine Phosphatases / antagonists & inhibitors
  • Protein Tyrosine Phosphatases / genetics*
  • Protein Tyrosine Phosphatases / metabolism*
  • Substrate Specificity

Substances

  • Enzyme Inhibitors
  • Mutant Proteins
  • Phosphopeptides
  • Protein Tyrosine Phosphatases