Vicinity analysis: a methodology for the identification of similar protein active sites

J Mol Model. 2009 May;15(5):489-98. doi: 10.1007/s00894-008-0424-7. Epub 2008 Dec 16.

Abstract

Vicinity analysis (VA) is a new methodology developed to identify similarities between protein binding sites based on their three-dimensional structure and the chemical similarity of matching residues. The major objective is to enable searching of the Protein Data Bank (PDB) for similar sub-pockets, especially in proteins from different structural and biochemical series. Inspection of the ligands bound in these pockets should allow ligand functionality to be identified, thus suggesting novel monomers for use in library synthesis. VA has been developed initially using the ATP binding site in kinases, an important class of protein targets involved in cell signalling and growth regulation. This paper defines the VA procedure and describes matches to the phosphate binding sub-pocket of cyclin-dependent protein kinase 2 that were found by searching a small test database that has also been used to parameterise the methodology.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Catalytic Domain
  • Catechol O-Methyltransferase / chemistry
  • Computational Biology / methods*
  • Cyclic AMP-Dependent Protein Kinases / chemistry
  • Cyclin-Dependent Kinase 2 / chemistry
  • Phosphates / chemistry
  • Proteins / chemistry*
  • ROC Curve
  • Staurosporine / chemistry

Substances

  • Phosphates
  • Proteins
  • Catechol O-Methyltransferase
  • Cyclic AMP-Dependent Protein Kinases
  • Cyclin-Dependent Kinase 2
  • Staurosporine