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The Three-Dimensional X-Ray Crystal Structure of HIV-1 Protease Complexed with a Hydroxyethylene Inhibitor

  • Bradford J. Graves
  • Marcos H. Hatada
  • Julann K. Miller
  • Mary C. Graves
  • Swapan Roy
  • Charles M. Cook
  • Antonin Kröhn
  • Joseph A. Martin
  • Noel A. Roberts
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 306)

Abstract

The aspartyl proteinase encoded within the genome of the type I human immunodeficiency virus (HIV-1 PR) is a valid and important target for the development of a therapeutic to treat HIV infections. Progress in this area has been rapid due to 1) the wealth of previous experience with other aspartyl proteinases and 2) the massive commitment by a large number of research groups worldwide. In this chapter we would like to discuss some of our efforts to develop a PR inhibitor by describing the structure of a complex between HIV-1 PR and a hydroxyethylene inhibitor. As a final note before continuing, we would like to acknowledge the significant contributions that Alex Wlodawer and his group have made to this field which have been important to the progress made not only by our group but by many others as well.

Keywords

Human Immunodeficiency Virus Aspartyl Proteinase Welwyn Garden City Human Renin Orthorhombic Form 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1991

Authors and Affiliations

  • Bradford J. Graves
    • 1
  • Marcos H. Hatada
    • 1
  • Julann K. Miller
    • 1
  • Mary C. Graves
    • 1
  • Swapan Roy
    • 1
  • Charles M. Cook
    • 1
  • Antonin Kröhn
    • 2
  • Joseph A. Martin
    • 2
  • Noel A. Roberts
    • 2
  1. 1.Roche Research CenterHoffmann-La Roche IncNutleyUSA
  2. 2.Roche Products LtdWelwyn Garden CityEngland

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