Conserved Folding in Retroviral Proteases: Crystal Structure of Synthetic HIV-1 Protease

The rational design of drugs that can inhibit the action of viral proteases depends on obtaining accurate structures

Alexander Wlodawer; Maria Miller; Mariusz Jaskólski; Bangalore K. Sathyanarayana; Eric Baldwin; Irene T. Weber; Linda M. Selk; Leigh Clawson; Jens Schneider; Stephen B. H. Kent

2006

Scholarcy highlights

  • The rational design of drugs that can inhibit the action of viral proteases depends on obtaining accurate structures
  • The crystal structure of chemically synthesized HIV-1 protease has been determined at 2.8 angstrom resolution with the use
  • of a model based on the Rous sarcoma virus protease structure
  • the cysteines were replaced by α-amino-n-butyric acid
  • The interface between the identical subunits forming the active protease dimer is composed of four well-ordered β strands
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