Crystal structures of human procathepsin B at 3.2 and 3.3 Angstroms resolution reveal an interaction motif between a papain-like cysteine protease and its propeptide

FEBS Lett. 1996 Apr 22;384(3):211-4. doi: 10.1016/0014-5793(96)00309-2.

Abstract

A wild-type human procathepsin B was expressed, crystallized in two crystal forms and its crystal structure determined at 3.2 and 3.3 Angstroms resolution. The structure reveals that the propeptide folds on the cathepsin B surface, shielding the enzyme active site from exposure to solvent. The structure of the enzymatically active domains is virtually identical to that of the native enzyme [Musil et al. (1991) EMBO J. 10, 2321-2330]: the main difference is that the occluding loop residues are lifted above the body of the mature enzyme, supporting the propeptide structure.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Cathepsin B / chemistry*
  • Cathepsin B / metabolism*
  • Crystallography, X-Ray*
  • Cysteine Endopeptidases / chemistry
  • Cysteine Endopeptidases / metabolism
  • Enzyme Precursors / chemistry*
  • Enzyme Precursors / metabolism*
  • Humans
  • Models, Molecular
  • Papain / chemistry
  • Papain / metabolism
  • Peptide Fragments / chemistry
  • Peptide Fragments / metabolism
  • Protein Conformation
  • Structure-Activity Relationship

Substances

  • Enzyme Precursors
  • Peptide Fragments
  • Cysteine Endopeptidases
  • procathepsin B
  • Cathepsin B
  • Papain