Campus Units
Biochemistry, Biophysics and Molecular Biology, Roy J. Carver Department of, Baker Center for Bioinformatics and Biological Statistics
Document Type
Article
Publication Version
Published Version
Publication Date
2005
Journal or Book Title
Journal of Biomolecular Structure and Dynamics
Volume
22
Issue
6
First Page
615
Last Page
624
DOI
10.1080/07391102.2005.10531228
Abstract
The association of a drug with its target protein has the effect of blocking the protein activity and is termed a promiscuous function to distinguish from the protein’s native function (Tawfik and associates, Nat. Genet. 37, 73-6, 2005). Obviously, a protein has not evolved naturally for drug association or drug resistance. Promiscuous protein functions exhibit unique traits of evolutionary adaptability, or evolvability, which is dependent on the induction of novel phenotypic traits by a small number of mutations. These mutations might have small effects on native functions, but large effects on promiscuous function; for example, an evolving protein could become increasingly drug resistant while maintaining its original function.
Rights
The authors, the publisher, and the right holders grant the right to use, reproduce, and disseminate the work in digital form to all users.
Copyright Owner
Taylor and Francis Group, LLC
Copyright Date
2005
Language
en
File Format
application/pdf
Recommended Citation
Fernandez, Ariel; Tawfik, Dan S.; Berkhout, Ben; Sanders, Rogier W.; Kloczkowski, Andrzej; Sen, Taner Z.; and Jernigan, Robert L., "Protein Promiscuity: Drug Resistance and Native Functions—HIV-1 Case" (2005). Biochemistry, Biophysics and Molecular Biology Publications. 167.
https://lib.dr.iastate.edu/bbmb_ag_pubs/167
Included in
Biochemistry Commons, Bioinformatics Commons, Biophysics Commons, Molecular Biology Commons, Structural Biology Commons
Comments
This article is published as Fernández, Ariel, Dan S. Tawfik, Ben Berkhout, Rogier Sanders, Andrzej Kloczkowski, Taner Sen, Bob Jernigan et al. "Protein promiscuity: drug resistance and native functions—HIV-1 case." Journal of Biomolecular Structure and Dynamics 22, no. 6 (2005): 615-624. doi: 10.1080/07391102.2005.10531228. Posted with permission.