Structural analysis of human immunodeficiency virus type 1 CRF01_AE protease in complex with the substrate p1-p6.
Authors
Bandaranayake, Rajintha M.Prabu-Jeyabalan, Moses
Kakizawa, Junko
Sugiura, Wataru
Schiffer, Celia A.
UMass Chan Affiliations
Department of Biochemistry and Molecular PharmacologyDocument Type
Journal ArticlePublication Date
2008-07-01Keywords
Amino Acid Sequence; Crystallization; Genetic Variation; HIV Protease; HIV-1; Hydrogen Bonding; Models, Molecular; Molecular Sequence Data; Protein Conformation; gag Gene Products, Human Immunodeficiency VirusLife Sciences
Medical Biochemistry
Medical Biophysics
Medicine and Health Sciences
Metadata
Show full item recordAbstract
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.Source
J Virol. 2008 Jul;82(13):6762-6. Link to article on publisher's websiteDOI
10.1128/JVI.00018-08Permanent Link to this Item
http://hdl.handle.net/20.500.14038/33046PubMed ID
18434392; 18434392Related Resources
Link to article in PubMedae974a485f413a2113503eed53cd6c53
10.1128/JVI.00018-08