Structural analysis of human immunodeficiency virus type 1 CRF01_AE protease in complex with the substrate p1-p6.
Department of Biochemistry and Molecular Pharmacology
Medical Subject Headings
Amino Acid Sequence; Crystallization; Genetic Variation; HIV Protease; HIV-1; Hydrogen Bonding; Models, Molecular; Molecular Sequence Data; Protein Conformation; gag Gene Products, Human Immunodeficiency Virus
Life Sciences | Medical Biochemistry | Medical Biophysics | Medicine and Health Sciences
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.
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Citation: J Virol. 2008 Jul;82(13):6762-6. Link to article on publisher's website
Bandaranayake, Rajintha M.; Prabu-Jeyabalan, Moses; Kakizawa, Junko; Sugiura, Wataru; and Schiffer, Celia A., "Structural analysis of human immunodeficiency virus type 1 CRF01_AE protease in complex with the substrate p1-p6." (2008). GSBS Student Publications. Paper 1595.