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Structural analysis of human immunodeficiency virus type 1 CRF01_AE protease in complex with the substrate p1-p6.


ABSTRACT: 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 A. 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.

SUBMITTER: Bandaranayake RM 

PROVIDER: S-EPMC2447101 | biostudies-literature | 2008 Jul

REPOSITORIES: biostudies-literature

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Structural analysis of human immunodeficiency virus type 1 CRF01_AE protease in complex with the substrate p1-p6.

Bandaranayake Rajintha M RM   Prabu-Jeyabalan Moses M   Kakizawa Junko J   Sugiura Wataru W   Schiffer Celia A CA  

Journal of virology 20080423 13


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 A. Hydrogen bonding between the flap hinge and the protease core regions shows significant structural rearrangements in CRF01_AE protease c  ...[more]

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