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Journal of Virology, July 2008, p. 6762-6766, Vol. 82, No. 13
0022-538X/08/$08.00+0 doi:10.1128/JVI.00018-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, 364 Plantation Street, Worcester, Massachusetts 01605,1 Laboratory of Therapeutic Research and Clinical Science, AIDS Research Center, National Institute of Infectious Diseases, 4-7-1 Gakuenn Musashimurayama, Tokyo 208-0011, Japan2
Received 3 January 2008/ Accepted 16 April 2008
The effect of amino acid variability between human immunodeficiency virus type 1 (HIV-1) clades on structure and the emergence of resistance mutations in HIV-1 protease has become an area of significant interest in recent years. We determined the first crystal structure of the HIV-1 CRF01_AE protease in complex with the p1-p6 substrate to a resolution of 2.8 Å. Hydrogen bonding between the flap hinge and the protease core regions shows significant structural rearrangements in CRF01_AE protease compared to the clade B protease structure.
Published ahead of print on 23 April 2008.
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