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.

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.

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

Language

en

File Format

application/pdf

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