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

Ligand binding by TPR domains.

Aitziber L Cortajarena1, Lynne Regan

  • 1Department of Molecular Biophysics & Biochemistry, Yale University, New Haven, Connecticut 06520, USA.

Protein Science : a Publication of the Protein Society
|April 28, 2006
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

Engineered protein nanoclusters reduce liver fibrosis and hepatocellular carcinoma in mice models.

Bioactive materials·2026
Same author

epiGPTope: A Machine Learning-Based Epitope Generator and Classifier.

ACS synthetic biology·2026
Same author

Magnetic nanoparticles as transducers for quick and direct virus detection in clinical samples.

Nanoscale·2025
Same author

Engineered Protein-Based Ionic Conductors for Sustainable Energy Storage Applications.

Advanced materials (Deerfield Beach, Fla.)·2025
Same author

Rational Crystal Contact Engineering for Programmable Self-Assembled Protein Architectures.

Angewandte Chemie (International ed. in English)·2025
Same author

SNUPN-Related Muscular Dystrophy: Novel Phenotypic, Pathological and Functional Protein Insights.

Annals of clinical and translational neurology·2025
Same journal

Macromolecular crowding inhibits degradation of alpha-synuclein amyloid fibrils induced by cathepsins and MMP9.

Protein science : a publication of the Protein Society·2026
Same journal

Sequence-encoded differences in the conformational ensembles of CITED transcriptional activation domains impact coactivator binding.

Protein science : a publication of the Protein Society·2026
Same journal

The phospholipid biosynthesis enzyme PlsB contains three distinct domains for membrane association, lysophosphatidic acid synthesis, and dimerization.

Protein science : a publication of the Protein Society·2026
Same journal

Structural basis of ligand selectivity in FAD/NAD(P)H-dependent dehydrogenases: insights from trypanothione reductase and type II NADH dehydrogenase.

Protein science : a publication of the Protein Society·2026
Same journal

Achieving protease substrate-specific inhibition by mAb dual functional selections.

Protein science : a publication of the Protein Society·2026
Same journal

How important are quantum mechanical effects in controlling biological functions: Enzymes, electron transfer and bird navigation.

Protein science : a publication of the Protein Society·2026
See all related articles

Tetratricopeptide repeat (TPR) domains bind peptide ligands without significant structural changes. Coupled folding and binding is not the common mechanism for TPR domain ligand recognition.

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Tetratricopeptide repeat (TPR) domains are known to bind specific peptide ligands.
  • TPR domains are implicated in mediating protein-protein interactions across various biological systems.

Purpose of the Study:

  • To compare peptide ligand-binding mechanisms across different TPR domains.
  • To investigate the structural rearrangements of TPR domains upon ligand binding.
  • To evaluate the proposed mechanism of coupled folding and binding in TPR domain ligand recognition.

Main Methods:

  • Comparative analysis of peptide ligand-binding.
  • Structural studies of TPR domains with and without bound ligands.

Main Results:

Related Experiment Videos

  • TPR domains exhibit minimal to no structural rearrangement upon binding to peptide ligands.
  • Specific examples illustrate conserved binding behavior across different TPR domains.
  • Data refutes the hypothesis that coupled folding and binding is a common recognition mechanism for TPR domains.

Conclusions:

  • TPR domain-ligand interactions are characterized by structural stability rather than induced fit.
  • The findings challenge existing models of TPR domain-mediated molecular recognition.
  • This work clarifies the mechanism of ligand binding for TPR domains in biological systems.