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

Using the Lac repressor system to identify interacting proteins.

N L Stricker1, P Schatz, M Li

  • 1Department of Neuroscience, School of Medicine, Johns Hopkins University, Baltimore, Maryland 21205, USA.

Methods in Enzymology
|June 1, 1999
PubMed
Summary

This study presents a protocol to identify peptides that bind to PDZ domains. These methods can be adapted to find interactions with other protein modules and guide further biochemical studies.

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

Tapping mode atomic force microscopy of hyaluronan: extended and intramolecularly interacting chains.

Biophysical journal·1998
Same author

Generation of purified neural precursors from embryonic stem cells by lineage selection.

Current biology : CB·1998
Same author

Amino acid residues that control pH modulation of transport-associated current in mammalian serotonin transporters.

The Journal of neuroscience : the official journal of the Society for Neuroscience·1998
Same author

Nonneural nuclear inclusions of androgen receptor protein in spinal and bulbar muscular atrophy.

The American journal of pathology·1998
Same author

Store-operated calcium entry promotes shape change in pulmonary endothelial cells expressing Trp1.

The American journal of physiology·1998
Same author

Nuclear inclusions of the androgen receptor protein in spinal and bulbar muscular atrophy.

Annals of neurology·1998

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Proteomics

Background:

  • PDZ domains are crucial protein interaction modules involved in diverse cellular processes.
  • Identifying specific peptide ligands for PDZ domains is essential for understanding protein complex formation and cellular signaling.
  • Existing methods for identifying PDZ-binding peptides can be labor-intensive and may lack broad applicability.

Purpose of the Study:

  • To develop and describe a robust protocol for identifying peptides that interact with PDZ domains.
  • To demonstrate the adaptability of the protocol for other purified protein modules or intact proteins.
  • To enable the prediction of potential protein-protein interactions based on sequence homology and experimental data.

Main Methods:

  • A series of experimental procedures designed to isolate and identify PDZ-binding peptides.

Related Experiment Videos

  • Utilizing sequence information and deduced consensus motifs to screen protein databases.
  • Cross-referencing predicted interactions with temporal and spatial expression data.

    • Main Results:

    • A validated protocol for identifying PDZ-interacting peptides.
    • Demonstration of the protocol's applicability to various protein modules.
    • Generation of consensus sequences that facilitate the identification of compatible protein candidates in databases.

    Conclusions:

    • The described protocol offers a versatile approach for discovering protein-protein interactions mediated by PDZ domains.
    • The method facilitates the identification of novel binding partners for PDZ domains and potentially other protein modules.
    • This work provides a foundation for designing targeted biochemical and molecular experiments to validate physical and functional interactions.