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Antimicrobial Agents and Chemotherapy, April 2006, p. 1518-1521, Vol. 50, No. 4
0066-4804/06/$08.00+0     doi:10.1128/AAC.50.4.1518-1521.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Substrate Envelope and Drug Resistance: Crystal Structure of RO1 in Complex with Wild-Type Human Immunodeficiency Virus Type 1 Protease

Moses Prabu-Jeyabalan,1 Nancy M. King,1 Ellen A. Nalivaika,1 Gabrielle Heilek-Snyder,2 Nick Cammack,2 and Celia A. Schiffer1*

Department of Biochemistry & Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts 01605,1 Roche, Palo Alto, California2

Received 22 July 2005/ Returned for modification 9 September 2005/ Accepted 12 January 2006

In our previous crystallographic studies of human immunodeficiency virus type 1 (HIV-1) protease-substrate complexes, we described a conserved "envelope" that appears to be important for substrate recognition and the selection of drug-resistant mutations. In this study, the complex of HIV-1 protease with the inhibitor RO1 was determined and comparison with the substrate envelope provides a rationale for mutational patterns.

* Corresponding author. Mailing address: Department of Biochemistry & Molecular Pharmacology, University of Massachusetts Medical School, 364 Plantation St., Worcester, MA 01605. Phone: (508) 856-8008. Fax: (508) 856-6464. E-mail: Celia.Schiffer{at}umassmed.edu.

Antimicrobial Agents and Chemotherapy, April 2006, p. 1518-1521, Vol. 50, No. 4
0066-4804/06/$08.00+0     doi:10.1128/AAC.50.4.1518-1521.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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Copyright © 2006 by the American Society for Microbiology. All rights reserved.