Apo and inhibitor complex structures of BACE (beta-secretase)

J Mol Biol. 2004 Oct 15;343(2):407-16. doi: 10.1016/j.jmb.2004.08.018.

Abstract

Human BACE, also known as beta-secretase, shows promise as a potential therapeutic target for Alzheimer's disease. We determined the apo structure of BACE to 1.75 A, and a structure of a hydroxyethylamine inhibitor complex derived by soaking. These show significant active-site movements compared to previously described BACE structures. Additionally, the structures reveal two pockets that could be targeted by structure-based drug design.

MeSH terms

  • Amines / chemistry*
  • Amines / metabolism
  • Amyloid Precursor Protein Secretases
  • Animals
  • Aspartic Acid Endopeptidases
  • Binding Sites
  • Crystallography, X-Ray
  • Drug Design
  • Endopeptidases / chemistry*
  • Endopeptidases / metabolism
  • Enzyme Inhibitors / chemistry*
  • Enzyme Inhibitors / metabolism
  • Humans
  • Hydrogen Bonding
  • Mice
  • Models, Molecular
  • Molecular Sequence Data
  • Molecular Structure
  • Protein Structure, Tertiary*
  • Temperature

Substances

  • Amines
  • Enzyme Inhibitors
  • Amyloid Precursor Protein Secretases
  • Endopeptidases
  • Aspartic Acid Endopeptidases
  • BACE1 protein, human
  • Bace1 protein, mouse

Associated data

  • PDB/1W50
  • PDB/1W51