Time Dependent Heterodimer Formation Leads to Inhibition of HIV Protease Activity

  • Lilia M. Babé
  • Charles S. Craik
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 306)


The protease encoded by the human immunodefiency virus (HIV) is a homodimer as determined by X-ray crystallographic (Navia et al., 1989, Wlodawer et al., 1989) and biochemical analysis (Meek et al., 1989). A four-stranded antiparallel ß-sheet generated by interdigitating N-and C-termini of the monomers dominates the dimer interface. This ß-sheet is partially stabilized by intersubunit backbone H-bonds of alternate amino acids from each of the four strands.


Human Immunodeficiency Virus Aspartyl Protease Human Immunodeficiency Virus Protease Alternate Amino Acid Active Human Immunodeficiency Virus 
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Copyright information

© Plenum Press, New York 1991

Authors and Affiliations

  • Lilia M. Babé
    • 1
  • Charles S. Craik
    • 1
  1. 1.Department of Pharmaceutical ChemistryUniversity of California, San FranciscoSan FranciscoUSA

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