Structure of human cathepsin D: comparison of inhibitor binding and subdomain displacement with other aspartic proteases

Adv Exp Med Biol. 1995:362:181-92. doi: 10.1007/978-1-4615-1871-6_22.
No abstract available

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Aspartic Acid Endopeptidases / antagonists & inhibitors
  • Aspartic Acid Endopeptidases / chemistry*
  • Aspartic Acid Endopeptidases / metabolism
  • Binding Sites
  • Binding, Competitive
  • Cathepsin D / antagonists & inhibitors
  • Cathepsin D / chemistry*
  • Cathepsin D / isolation & purification
  • Crystallization
  • Crystallography, X-Ray
  • Humans
  • Hydrogen Bonding
  • Liver / enzymology
  • Macromolecular Substances
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Structure, Secondary*
  • Sequence Homology, Amino Acid
  • Swine

Substances

  • Macromolecular Substances
  • Aspartic Acid Endopeptidases
  • Cathepsin D