U.S. Department of Health and Human Services
 

 Contact Info

 
Tel: 301-496-9893
Email: jmsayer@niddk.nih.gov
 

 Select Experience

 
  • Research ChemistLCP, NIDDK, NIH2007-present
  • Research ChemistLBC, NIDDK, NIH1985-2007
  • Special ExpertLBC, NIDDK, NIH1979-1985
  • Guest WorkerLBC, NIDDK, NIH1979-1983
  • Senior Research AssociateBrandeis University1969- 1974
  • NIH Postdoctoral FellowBrandeis University1967-1969
  • Ph.D.Yale University1967
 

 Related Links

 

    Jane M. Sayer, Ph.D.

    Research Chemist, Office of the Chief, Laboratory of Chemical Physics
    Specialties
    • Chemistry/Chemical Biology
    • Molecular Biology/Biochemistry

    ​Research Images

    Images or videos appear below. Clicking images or videos provides an expanded view.

    TitleDescriptionImage
    A natural PR variant that resembles biochemically the predominant PRM bears 20 amino acid substitutions differing markedly from those of a multi-drug resistant mutant.Sequences of natural HIV-1 PR variants (groups M, N, O, and P) are compared with an extreme drug-resistant mutant, PR20.  Seven mutations (red) associated with major drug resistance are not present in the natural variants and cluster near highly conserved regions (gold) essential for enzyme functionality.A natural PR variant that resembles biochemically the predominant PRM bears 20 amino acid substitutions differing markedly from those of a multi-drug resistant mutant.Enlarge
    Comparison of clinical inhibitor binding to PR and mammalian pepsin.The image depicts three clinical inhibitors of HIV-1 PR, darunavir, amprenavir, and ritonavir, inhibit pepsin, a mammalian aspartyl protease, at low micromolar concentrations.   This model based on crystal structures suggests a possible binding mode of amprenavir to pepsin.  Serine residues 36 and 219 of pepsin take the place of Asp 29’ and 29 of PR.Comparison of clinical inhibitor binding to PR and mammalian pepsin.Enlarge