GSBS Student Publications


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

UMMS Affiliation

Department of Biochemistry and Molecular Pharmacology



Document Type


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.

Rights and Permissions

Citation: J Virol. 2008 Jul;82(13):6762-6. Link to article on publisher's website

DOI of Published Version


Related Resources

Link to article in PubMed

Journal Title

Journal of virology

PubMed ID