Targeting Protein Multiple Conformations: A Structure-Based Strategy for Kinase Drug Design | Bentham Science
Generic placeholder image

Current Topics in Medicinal Chemistry

Editor-in-Chief

ISSN (Print): 1568-0266
ISSN (Online): 1873-4294

Targeting Protein Multiple Conformations: A Structure-Based Strategy for Kinase Drug Design

Author(s): Liao Jie-Lou Jeffrey and Andrews C. Robert

Volume 7, Issue 14, 2007

Page: [1394 - 1407] Pages: 14

DOI: 10.2174/156802607781696783

Price: $65

Open Access Journals Promotions 2
Abstract

Multiple conformations of a protein kinase target offer an opportunity to design small-molecule inhibitors with distinct but clinically useful profiles. This article analyzes and classifies the binding pockets in the kinase catalytic cleft in different conformational states. Targeting kinase multiple conformations as an emerging strategy in the field is exemplified with important small-molecule agents in the clinic. The structure-based analysis in the paper provides a rationale for thwarting the development of drug-resistant mutations in antikinase therapy.

Keywords: Protein kinase, multiple conformations, catalytic cleft, binding pocket, DFG motif, αC helix, protein kinase inhibitor, resistant mutation


Rights & Permissions Print Cite
© 2024 Bentham Science Publishers | Privacy Policy