Homology modeling of Entamoeba histolytica cysteine proteinases reveals the basis for cathepsin L-like structure with cathepsin B-like specificity

Arch Med Res. Jul-Aug 2000;31(4 Suppl):S63-4. doi: 10.1016/s0188-4409(00)00154-5.
No abstract available

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cathepsin B / metabolism*
  • Cathepsin L
  • Cathepsins / chemistry*
  • Cysteine Endopeptidases / chemistry
  • Cysteine Endopeptidases / metabolism*
  • Endopeptidases*
  • Entamoeba histolytica / enzymology*
  • Molecular Sequence Data
  • Sequence Homology, Amino Acid
  • Substrate Specificity

Substances

  • Cathepsins
  • Endopeptidases
  • Cysteine Endopeptidases
  • Cathepsin B
  • Cathepsin L