Skip to content
2000
Volume 5, Issue 4
  • ISSN: 1573-4099
  • E-ISSN: 1875-6697

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.

Loading

Article metrics loading...

/content/journals/cad/10.2174/157340909789577874
2009-12-01
2025-05-24
Loading full text...

Full text loading...

/content/journals/cad/10.2174/157340909789577874
Loading
This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error
Please enter a valid_number test