Geometry of GPPE binding to picrate and to the urokinase type plasminogen activator

Bioorg Med Chem Lett. 2007 Nov 15;17(22):6212-5. doi: 10.1016/j.bmcl.2007.09.020. Epub 2007 Sep 8.

Abstract

Crystal structure of 2-(4-guanidynephenyl)-1-phenyl-ethanone (GPPE) in two different environments was determined in order to compare the binding geometry of these compound to a simple picrate anion and to protein, urokinase-type plasminogen activator (uPA), which may be treated as a target for anti-cancer drugs. It was shown that the conformation and the hydrogen-bonding formation by GPPE molecule are similar in both environments, but several important differences were discovered and described.

MeSH terms

  • Anions
  • Binding Sites / drug effects
  • Crystallography, X-Ray
  • Guanidines / chemistry*
  • Guanidines / metabolism
  • Hydrogen Bonding
  • Models, Molecular
  • Molecular Structure
  • Picrates / chemistry*
  • Picrates / metabolism
  • Protein Binding
  • Protein Structure, Tertiary
  • Urokinase-Type Plasminogen Activator / chemistry*
  • Urokinase-Type Plasminogen Activator / metabolism

Substances

  • 2-(4-guanidynephenyl)-1-phenyl-ethanone
  • Anions
  • Guanidines
  • Picrates
  • picric acid
  • Urokinase-Type Plasminogen Activator