title: Structural studies of the acquired immunodeficiency syndrome virus reverse transcriptase.
abstract: The clinical success of zidovudine has established the human immunodeficiency virus (HIV) reverse transcriptase (RT) as a valid target for the design of drugs to treat acquired immunodeficiency syndrome. In order to facilitate structural studies of this enzyme, expression systems in Escherichia coli, which allow the production of large amounts of RT, have been established. Using this recombinant material the RT has been purified and crystallized. Crystallographic studies currently underway are aimed at elucidating the three-dimensional structure of HIV RT. The availability of a bacterial expression system has enabled structural/functional studies of the RT by site-directed mutagenesis. These studies have identified amino acid residues that are essential for activity of the enzyme and might be involved in substrate binding. It is hoped that structural information of this nature will allow the rational design of HIV RT inhibitors.
authors: Wellcome Research Laboratories, Langley Court, Beckenham, Kent, United Kingdom.
authors: B A
authors: BA
authors: Larder
authors: D J
authors: DJ
authors: Purifoy
authors: K L
authors: KL
authors: Powell
authors: C
authors: C
authors: Bradley
authors: S
authors: S
authors: Kemp
authors: M
authors: M
authors: Tisdale
authors: P
authors: P
authors: Ertl
authors: G K
authors: GK
authors: Darby
authors: D
authors: D
authors: Stammers
mesh_terms: D000998:Antiviral Agents; D055598:Chemical Phenomena; D002621:Chemistry; D004926:Escherichia coli; D006678:HIV / Q000201:enzymology*; D006801:Humans; D012194:RNA-Directed DNA Polymerase / Q000032:analysis*; D011994:Recombinant Proteins / Q000032:analysis
chemical_list: D000998:Antiviral Agents; D011994:Recombinant Proteins; D012194:RNA-Directed DNA Polymerase