Ligand-receptor 3-D similarity studies using multiple 4-point pharmacophores

Pac Symp Biocomput. 1999:456-67. doi: 10.1142/9789814447300_0045.

Abstract

A new method for 3-D similarity is presented based on the multiple potential 4-point 3-D pharmacophores expressed by ligands and complementary to receptors. These are calculated for ligands taking conformational flexibility into account, and for receptors through the use of complementary site-points. Through this common frame of reference both ligand-ligand and ligand-receptor similarity studies are possible. The application of the method to selectivity between different serine proteases (thrombin, factor Xa and trypsin) is discussed, and the need to use 4-point pharmacophores rather than 3-point pharmacophores is illustrated. A novel refinement to the potential pharmacophore method that uses a "special" feature to give a relative measure of similarity/diversity is also discussed.

Publication types

  • Comparative Study

MeSH terms

  • Computer Graphics*
  • Drug Design*
  • Factor Xa / chemistry
  • Factor Xa / metabolism
  • Ligands*
  • Models, Molecular
  • Protein Conformation
  • Receptors, Drug / chemistry*
  • Receptors, Drug / metabolism*
  • Serine Endopeptidases / chemistry*
  • Serine Endopeptidases / metabolism*
  • Serine Proteinase Inhibitors / chemistry
  • Software*
  • Thrombin / chemistry
  • Thrombin / metabolism
  • Trypsin / chemistry
  • Trypsin / metabolism

Substances

  • Ligands
  • Receptors, Drug
  • Serine Proteinase Inhibitors
  • Serine Endopeptidases
  • Trypsin
  • Thrombin
  • Factor Xa