Structural and biochemical studies of retroviral proteases.
Retroviral proteases form a unique subclass of the family of aspartic proteases. These homodimeric enzymes from a number of viral sources have by now been extensively characterized, both structurally and biochemically. The importance of such knowledge to the development of new drugs against AIDS has been, to a large extent, the driving force behind this progress. High-resolution structures are now available for enzymes from human immunodeficiency virus types 1 and 2, simian immunodeficiency virus, feline immunodeficiency virus, Rous sarcoma virus, and equine infectious anemia virus. In this review, structural and biochemical data for retroviral proteases are compared in order to analyze the similarities and differences between the enzymes from different sources and to enhance our understanding of their properties.
Wlodawer
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Macromolecular Crystallography Laboratory, Program in Structural Biology, NCI-Frederick Cancer Research and Development Center, Frederick, MD 21702, USA. wlodawer@ncifcrf.gov
Gustchina
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D000595:Amino Acid Sequence; D001358:Avian Sarcoma Viruses; D001665:Binding Sites; D010450:Endopeptidases / Q000737:chemistry / Q000378:metabolism*; D004791:Enzyme Inhibitors / Q000737:chemistry; D015497:HIV-1; D015498:HIV-2; D016089:Immunodeficiency Virus, Feline; D004860:Infectious Anemia Virus, Equine; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D012190:Retroviridae / Q000201:enzymology*; D016415:Sequence Alignment; D015302:Simian Immunodeficiency Virus; D013379:Substrate Specificity
D004791:Enzyme Inhibitors; D010450:Endopeptidases