Skip to main content
SpringerLink
Log in

Studies of the Autoprocessing of the HIV-1 Protease Using Cleavage Site Mutants

  • Chapter
Structure and Function of the Aspartic Proteinases

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 306))

Abstract

The distinguishing features of aspartyl proteases in retroviruses, vis à vis the semi-symmetrical aspartyl proteases in other organisms, is the paucity of the genetic information in the viruses sufficient for the synthesis of a monomelic protein, from which the homodimer is assembled with the formation of the characteristic active site structure.1

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution
Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 39.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 54.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. A. Wlodawer, M. Miller, M. Jaskólski, B. K. Sathyanarayana, E. Baldwin, I. T. Weber, L. M. Selk, L. Clawson, J. Schneider and S. B. H. Kent, Conserved folding in retroviral proteases: crystal structure of a synthetic HIV-1 protease, Science 245: 616 (1989).

    Article  PubMed  CAS  Google Scholar 

  2. J. M. Louis, E. M. Wondrak, T. D. Copeland, C. A. D. Smith, P. T. Mora and S. Oroszlan, Chemical synthesis and expression of the HIV-1 protease gene in E. coli, Biochem. Biophys. Res. Comm. 159: 87 (1989).

    Article  PubMed  CAS  Google Scholar 

  3. J. M. Louis, C. A. D. Smith, E. M. Wondrak, P. T. Mora and S. Oroszlan, Substitution mutations of the highly conserved Arginine 87 of HIV-1 protease results in loss of proteolytic activity, Biochem. Biophys. Res. Comm. 164: 30 (1989).

    Article  PubMed  CAS  Google Scholar 

  4. C. Guan, P. Li, P. D. Riggs and H. Inouye, Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein, Gene 67: 21 (1988).

    Article  PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Laboratory of Cellular and Developmental Biology, NIDDK, NIH, Bethesda, Maryland, 20892, USA

    John M. Louis

  2. Laboratory of Molecular Virology and Carcinogenesis, ABL-Basic Research Program, NCI-FCRDC, Frederick, Maryland, 21701, USA

    Stephen Oroszlan

  3. Office of the Director, DCBD, NCI, NIH, Bethesda, Maryland, 20892, USA

    Peter T. Mora

Authors
  1. John M. Louis
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Stephen Oroszlan
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Peter T. Mora
    View author publications

    You can also search for this author in PubMed Google Scholar

Editor information

Editors and Affiliations

  1. University of Florida-College of Medicine, Gainesville, Florida, USA

    Ben M. Dunn

Rights and permissions

Reprints and permissions

Copyright information

© 1991 Plenum Press, New York

About this chapter

Cite this chapter

Louis, J.M., Oroszlan, S., Mora, P.T. (1991). Studies of the Autoprocessing of the HIV-1 Protease Using Cleavage Site Mutants. In: Dunn, B.M. (eds) Structure and Function of the Aspartic Proteinases. Advances in Experimental Medicine and Biology, vol 306. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-6012-4_64

Download citation

  • DOI: https://doi.org/10.1007/978-1-4684-6012-4_64

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4684-6014-8

  • Online ISBN: 978-1-4684-6012-4

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics

Search

Navigation