Mutations in the QVVAG region of the cysteine proteinase inhibitor stefin B

Biol Chem Hoppe Seyler. 1990 May:371 Suppl:157-60.

Abstract

Variants of human stefin B were constructed by cassette mutagenesis. Val47 as the constituent of highly conserved QVVAG sequence was substituted by hydrophobic amino acids of increasing size - Ala, Ile and Phe. Recombinant proteins were expressed in E. coli and Ki values for papain were determined. Substitutions did not cause a major change in Ki value and we conclude that the interaction with the proteinases is not the reason for the conservation of the pentapeptide.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Base Sequence
  • Cloning, Molecular
  • Cystatin B
  • Cystatins / biosynthesis
  • Cystatins / genetics*
  • Cysteine Proteinase Inhibitors*
  • Humans
  • Molecular Sequence Data
  • Mutation*
  • Papain / genetics
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / genetics

Substances

  • CSTB protein, human
  • Cystatins
  • Cysteine Proteinase Inhibitors
  • Recombinant Proteins
  • Cystatin B
  • Papain