Current Computer-Aided Drug Design

Subhash C. Basak
Departments of Chemistry, Biochemistry & Molecular Biology University of Minnesota Duluth
Duluth, MN 55811


Calmodulin in Complex with Proteins and Small Molecule Ligands: Operating with the Element of Surprise; Implications for Structure-Based Drug Design

Author(s): Dora K. Menyhard, Gyorgy M. Keseru, Gabor Naray-Szabo.


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.

Keywords: Calmodulin, protein interactions, small molecule binding, hydrophobicity, amphiphilicity, drug design

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Article Details

Year: 2009
Page: [264 - 279]
Pages: 16
DOI: 10.2174/157340909789577874
Price: $58