Tyrosine kinase drug discovery: What can be learned from solved crystal structures?

Loris Moretti, Laura Tchernin, Leonardo Scapozza

Research output: Contribution to journalArticlepeer-review

Abstract

Understanding molecular recognition during ligand binding is crucial for rational drug design. Protein kinases are a well known pharmacological target, especially in the therapeutic area of cancer. Solved crystal structures of tyrosine kinase domains in complex with ligands deliver insight into the binding event. These experimental data were collected and analysed by means of molecular modelling techniques. Common molecular recognition patterns were depicted and studied among this class of proteins. The results of this analysis and the consequences for rational design of inhibitors are presented.

Original languageEnglish
Pages (from-to)38-49
Number of pages12
JournalArkivoc
Volume2006
Issue number8
Publication statusPublished - May 18 2006

Keywords

  • Inhibitor minimal requirements and conserved ligand-kinase interactions
  • Ligand core
  • Molecular modelling
  • Tyrosine kinase ligands

ASJC Scopus subject areas

  • Organic Chemistry

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