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2.3 Å crystal structure of a drug resistant HIV C N88D/L90M protease complexed with Saquinavir

The HIV C‐N88D/L90M drug resistant variant of HIV C protease has been previously engineered and shown to exhibit a 42 fold increase in Ki value for saquinavir (SQV) compared to the wild‐type enzyme. In an effort to explain the sizable decrease in binding affinity to saquinavir observed with this variant, we have solved the crystal structure for the HIV C‐N88D/L90M variant complexed with saquinavir at 2.3 Å resolution. These data will be useful in identifying key molecular interactions involved in mediating drug binding in the active site of the protease. Additionally, this information will be useful in the subsequent structure‐based drug design of novel HIV protease inhibitors effective against drug resistant strains of HIV. Supported by NIH grant AI28571‐22.