Mark Knapp, Cornelia Bellamacina, Jeremy M. Murray and Dirksen E. Bussiere Pages 1129 - 1159 ( 31 )
Purine-binding proteins are of critical importance to all living organisms. Approximately 13% of the human genome is devoted to coding for purine-binding proteins. Given their importance, purine-binding proteins are attractive targets for chemotherapeutic intervention against a variety of disease states, particularly cancer. Modern computational and biophysical techniques, combined together in a structure-based drug design approach, aid immensely in the discovery of inhibitors of these targets. This review covers the process of modern structure-based drug design and gives examples of its use in discovery and development of drugs that target purine-binding proteins. The targets reviewed are human purine nucleoside phosphorylase, human epidermal growth factor receptor kinase, and human kinesin spindle protein.
Structure-based drug design, purine-binding proteins, structural biology, Eg5, KSP, kinases, purine nucleoside phosphorylase, PNP
Chiron Corporation,Computational Chemistry and Structural Chemistry, Biopharma Research,4560 Horton Street, M/S 4.4, Emeryville, CA 94608-2916.