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 Concept Videos

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

10.0K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
10.0K
Inhibitors of Viral Protein Synthesis01:30

Inhibitors of Viral Protein Synthesis

47
Protein synthesis is indispensable for viral replication, as viruses lack the cellular machinery required for this process and must hijack the host's translational apparatus. In response, host cells deploy a critical innate immune defense involving interferons, specialized cytokines that play a central role in inhibiting viral propagation.Upon viral detection, infected cells release interferons that bind to receptors on adjacent uninfected cells, activating the JAK-STAT signaling pathway and...
47

You might also read

Related Articles

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

Sort by
Same author

T cell epitope engineering: an avian H7N9 influenza vaccine strategy for pandemic preparedness and response.

Human vaccines & immunotherapeutics·2018
Same author

Substrate sequence selectivity of APOBEC3A implicates intra-DNA interactions.

Scientific reports·2018
Same author

Transcriptomic signature predicts the distant relapse in patients with ER+ breast cancer treated with tamoxifen for five years.

Molecular medicine reports·2017
Same author

Transgenic Bt cotton expressing Cry1Ac/Cry2Ab or Cry1Ac/EPSPS does not affect the plant bug Adelphocoris suturalis or the pollinating beetle Haptoncus luteolus.

Environmental pollution (Barking, Essex : 1987)·2017
Same author

Discovery of the leinamycin family of natural products by mining actinobacterial genomes.

Proceedings of the National Academy of Sciences of the United States of America·2017
Same author

Assessment of the neuropsychiatric comorbidities in Chinese children with epilepsy using the MINI-KID tool.

Epilepsy research·2017

Related Experiment Video

Updated: Apr 19, 2026

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding
10:50

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding

Published on: September 15, 2010

10.0K

Modulation of HIV protease flexibility by the T80N mutation.

Hao Zhou1, Shangyang Li1, John Badger2

  • 1Department of Electrical and Computer Engineering, Northeastern University, Boston, Massachusetts.

Proteins
|December 10, 2014
PubMed
Summary

HIV protease flexibility is crucial for its function. A mutation at Thr80 significantly reduces enzyme flexibility, impacting catalytic activity and highlighting the importance of protein-wide dynamics for HIV protease function.

Keywords:
molecular dynamics simulationprotein flexibilityx-ray solution scattering

More Related Videos

Amplification of Near Full-length HIV-1 Proviruses for Next-Generation Sequencing
10:18

Amplification of Near Full-length HIV-1 Proviruses for Next-Generation Sequencing

Published on: October 16, 2018

12.9K
Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods
10:40

Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods

Published on: December 21, 2019

26.6K

Related Experiment Videos

Last Updated: Apr 19, 2026

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding
10:50

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding

Published on: September 15, 2010

10.0K
Amplification of Near Full-length HIV-1 Proviruses for Next-Generation Sequencing
10:18

Amplification of Near Full-length HIV-1 Proviruses for Next-Generation Sequencing

Published on: October 16, 2018

12.9K
Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods
10:40

Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods

Published on: December 21, 2019

26.6K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • HIV protease (HIVp) flexibility is essential for enzymatic activity and substrate binding.
  • While flap flexibility is recognized, other regions, like the Thr80 loop, also critically influence function.
  • The conserved Thr80 residue is vital, as its mutation (T80N) abolishes catalytic activity while maintaining structural integrity.

Purpose of the Study:

  • To investigate the impact of the T80N mutation on HIV protease flexibility.
  • To determine how alterations in flexibility affect the enzyme's overall dynamics and function.

Main Methods:

  • Wide-angle X-ray scattering (WAXS) was employed to measure flexibility in HIVp variants.
  • Experimental WAXS data was compared with theoretical patterns derived from rigid atomic models.
  • Analytic methods were used to analyze modulations in intensity distribution due to protein structural fluctuations.

Main Results:

  • The T80N mutation resulted in a significantly more rigid HIV protease compared to wild-type (WT) across all length scales.
  • This single point mutation induced widespread effects, altering the mobility of amino acids within the enzyme's core.
  • The observed rigidity in the T80N variant correlated with the complete loss of catalytic activity.

Conclusions:

  • Protein flexibility is not localized but extends throughout HIV protease.
  • The Thr80 residue plays a critical role in maintaining the dynamic properties necessary for HIV protease function.
  • Targeting protein dynamics, beyond the active site, offers potential avenues for therapeutic intervention against HIV.