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

Sequence-specific dynamics modulate recognition specificity in WW domains.

Tao Peng1, John S Zintsmaster, Andrew T Namanja

  • 1Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556 USA.

Nature Structural & Molecular Biology
|March 6, 2007
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

Ionizable networks mediate pH-dependent allostery in the SH2 domain-containing signaling proteins SHP2 and SRC.

Science signaling·2025
Same author

Beyond Isotopic Labeling: Expanding the Reach of Protein-Detect NMR in Lead Discovery.

ACS medicinal chemistry letters·2025
Same author

Bacterial Phosphorylation Suppresses Carbapenemase Activity of the Class-D β-Lactamase OXA-24/40 from <i>Acinetobacter baumannii</i>.

Journal of the American Chemical Society·2024
Same author

Pin1 WW Domain Ligand Library Synthesized with an Easy Solid-Phase Phosphorylating Reagent.

Biochemistry·2024
Same author

Ionizable networks mediate pH-dependent allostery in SH2 signaling proteins.

bioRxiv : the preprint server for biology·2024
Same author

Mixed Ligand Passivation as the Origin of Near-Unity Emission Quantum Yields in CsPbBr<sub>3</sub> Nanocrystals.

Journal of the American Chemical Society·2023
Same journal

Promoter reinforcement supports transcriptional resilience in drug-resistant cancer.

Nature structural & molecular biology·2026
Same journal

Publisher Correction: Interplay between cohesin and RNA polymerase II in regulating chromatin interactions and gene transcription.

Nature structural & molecular biology·2026
Same journal

An asymmetric non-canonical nucleosome shapes the directionality of transcription outcomes.

Nature structural & molecular biology·2026
Same journal

Structural insights into neurokinin 2 receptor selectivity hold implications for obesity therapeutics.

Nature structural & molecular biology·2026
Same journal

Genome-wide absolute quantification of chromatin looping.

Nature structural & molecular biology·2026
Same journal

Putting numbers on chromatin looping.

Nature structural & molecular biology·2026
See all related articles

Protein recognition relies on more than just chemical properties. Intrinsic flexibility in WW domain loops is key to specificity, with changes affecting ligand binding.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Protein-recognition motifs typically bind ligands via specific chemical properties of amino acid sequences.
  • The role of intrinsic dynamics in the specificity of these interactions is not fully understood.

Purpose of the Study:

  • To investigate the role of intrinsic flexibility in the binding specificity of WW domains.
  • To determine if dynamic modes, beyond chemical composition, are selected for in recognition motifs.

Main Methods:

  • Studied a specific WW domain and its interaction with ligands.
  • Utilized mutational analysis, specifically a single-residue deletion in a flexible loop.
  • Assessed changes in loop flexibility and ligand binding affinity.

Related Experiment Videos

Main Results:

  • Identified an intrinsically flexible loop as crucial for WW domain specificity.
  • Demonstrated that a single-residue deletion reduced both loop flexibility and ligand binding affinity.
  • Showed that this loop partially rigidifies upon ligand docking.

Conclusions:

  • Binding specificity of protein-recognition motifs is influenced by intrinsic dynamic properties, not solely chemical moieties.
  • Natural selection may favor sequences that optimize both chemical properties and dynamic modes for enhanced specificity.
  • This finding offers a new perspective on the evolution and design of protein-recognition systems.