Structural and biochemical studies of retroviral proteases

Citation
A. Wlodawer et A. Gustchina, Structural and biochemical studies of retroviral proteases, BBA-PROT ST, 1477(1-2), 2000, pp. 16-34
Citations number
107
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY
ISSN journal
01674838 → ACNP
Volume
1477
Issue
1-2
Year of publication
2000
Pages
16 - 34
Database
ISI
SICI code
0167-4838(20000307)1477:1-2<16:SABSOR>2.0.ZU;2-K
Abstract
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 . (C) 2000 Elsevier Science B.V. All rights reserved.