Calmodulin in complex with proteins and small molecule ligands: Operating with the element of surprise; implications for structure-based drug design

Dóra K. Menyhárd, György M. Keserucombining double acute accent, Gábor Náray-Szabó

Research output: Contribution to journalReview article

9 Citations (Scopus)

Abstract

Calmodulin plays a role in several life processes, its flexibility allows binding of a number of different ligands from small molecules to amphiphilic peptide helices and proteins. Through the diversity of its functions, it is quite difficult to find new drugs, which bind to calmodulin as a target. We present available structural information on the protein, obtained by X-ray diffraction, nuclear magnetic resonance spectroscopy and molecular modeling and try to derive some conclusions on structure-activity relationships.

Original languageEnglish
Pages (from-to)264-279
Number of pages16
JournalCurrent Computer-Aided Drug Design
Volume5
Issue number4
DOIs
Publication statusPublished - Dec 1 2009

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Keywords

  • Amphiphilicity
  • Calmodulin
  • Drug design
  • Hydrophobicity
  • Protein interactions
  • Small molecule binding

ASJC Scopus subject areas

  • Molecular Medicine
  • Drug Discovery

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