Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Retroviral proteases.

Ben M Dunn1, Maureen M Goodenow, Alla Gustchina

  • 1Department of Biochemistry and Molecular Biology, University of Florida, Gainesville, FL 32610, USA. bdunn@college.med.ufl.edu

Genome Biology
|May 2, 2002
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Lysozyme revisited: evaluating models of a reference protein in structural biology.

Current research in structural biology·2026
Same author

Impact of Single Halogen Atom Substitutions on Antiviral Profile of Inhibitors Targeting SARS-CoV‑2 Main Protease.

ACS omega·2026
Same author

How to mitigate the caveat emptor burden of human and machine users of the Protein Data Bank.

Acta crystallographica. Section D, Structural biology·2026
Same author

A Critical Look at the Crystal Structures of cAMP-Dependent Protein Kinases.

Kinases and phosphatases·2025
Same author

Multi-Modal Profiling Reveals Contrasting Immunomodulatory Effects of Recreational Marijuana Used Alone or with Tobacco in Youth with HIV.

Cells·2025
Same author

The Role of Microarray in Modern Sequencing: Statistical Approach Matters in a Comparison Between Microarray and RNA-Seq.

Biotech (Basel (Switzerland))·2025
Same journal

Somatic mobility of transposons is explosive and shaped by distinct integration biases in Arabidopsis thaliana.

Genome biology·2026
Same journal

UK Biobank whole-genome sequencing reveals robust contributions of rare variants to complex-trait heritability.

Genome biology·2026
Same journal

A one-week automated genome-wide optical pooled screen using OttoSeq.

Genome biology·2026
Same journal

Integrated lipidomic and transcriptomic profiling of the host response in human malaria.

Genome biology·2026
Same journal

Centromeric satellite expansion drives genome evolution in the snowy owl.

Genome biology·2026
Same journal

Mapping the landscape of allele-specific expression in porcine genomes.

Genome biology·2026
See all related articles

Retroviral proteases are essential for viral replication and share structural similarities with aspartic peptidases. Understanding their variations is crucial for developing new therapies against viruses like HIV.

Area of Science:

  • Molecular Biology
  • Virology
  • Biochemistry

Background:

  • Retroviral proteases are critical enzymes in the replication cycle of various retroviruses, including human immunodeficiency virus (HIV).
  • These proteases are synthesized as polyprotein precursors and function by cleaving specific sites to release mature viral proteins.
  • They belong to the aspartic peptidase family and exist as active homodimers.

Purpose of the Study:

  • To elucidate the structural and functional characteristics of retroviral proteases.
  • To highlight the significance of retroviral proteases in viral propagation and disease.
  • To underscore the importance of studying protease variations for therapeutic drug development.

Main Methods:

  • Structural analysis of retroviral protease monomers and dimers.

Related Experiment Videos

  • Comparison with aspartic peptidases.
  • Examination of gene sequence variations and their impact on protease function.
  • Main Results:

    • Retroviral proteases are homodimers, each monomer comprising two hairpin loops, a catalytic loop with aspartic acid, and an alpha helix.
    • Structural similarity was identified between retroviral proteases and single-chain aspartic peptidases.
    • Mutations in protease binding clefts or cleavage sites can affect drug efficacy.

    Conclusions:

    • Retroviral proteases, including those from HIV, are a conserved family with implications across various retroviruses and even some retrotransposons.
    • Understanding the structural basis and sequence variability of these proteases is fundamental for combating viral infections.
    • Continued research into retroviral proteases is vital for the development of novel antiviral therapeutics, particularly for HIV.