Retroviral proteases form a unique subclass of the family of aspartic prote
ases. These homodimeric enzymes from a number of viral sources have by now
been extensively characterized, both structurally and biochemically. The im
portance of such knowledge to the development of new drugs against AIDS has
been, to a large extent, the driving force behind this progress. High-reso
lution structures are now available for enzymes from human immunodeficiency
virus types 1 and 2. simian immunodeficiency virus. feline immunodeficienc
y virus, Rous sarcoma virus. and equine infectious anemia virus. In this re
view. structural and biochemical data for retroviral protrases are compared
in order to analyze the similarities and differences between the enzymes f
rom different sources and to enhance our understanding of their propel-ties
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