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

Adaptors and integrators

D Cowburn1

  • 1The Rockefeller University, 1230 York Avenue, New York, NY 10021-6399, USA. cowburn@rockvax.rockefeller.edu

Structure (London, England : 1993)
|September 15, 1996
PubMed
Summary
This summary is machine-generated.

The PTB domain expands the PH-domain set and peptide-protein recognition motifs. The PDZ domain exhibits a notable resemblance to these structures.

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

Integrating NOE and RDC using sum-of-squares relaxation for protein structure determination.

Journal of biomolecular NMR·2017
Same author

A peptide mimic blocks the cross-reaction of anti-DNA antibodies with glomerular antigens.

Clinical and experimental immunology·2015
Same author

Novel mechanism of regulation of the non-receptor protein tyrosine kinase Csk: insights from NMR mapping studies and site-directed mutagenesis.

Journal of molecular biology·2001
Same author

A novel, specific interaction involving the Csk SH3 domain and its natural ligand.

Nature structural biology·2001
Same author

Peptide chemical ligation inside living cells: in vivo generation of a circular protein domain.

Bioorganic & medicinal chemistry·2001
Same author

Nuclear magnetic resonance relaxation in determination of residue-specific 15N chemical shift tensors in proteins in solution: protein dynamics, structure, and applications of transverse relaxation optimized spectroscopy.

Methods in enzymology·2001
Same journal

Structure of Perinereis linea erythrocruorin reveals a compact extracellular globin megacomplex.

Structure (London, England : 1993)·2026
Same journal

Meet the author: Stephen Brohawn.

Structure (London, England : 1993)·2026
Same journal

Tetraspanins bring Norrin into focus: Structural insights into ligand-specific Wnt signaling.

Structure (London, England : 1993)·2026
Same journal

Uncovering subtype-selective activation of the K<sub>Ca</sub>3.1 channel by SKA-111.

Structure (London, England : 1993)·2026
Same journal

Identification and structure determination of a type III-Bv CRISPR complex that post-translationally modifies an associated toxin.

Structure (London, England : 1993)·2026
Same journal

Cryo-EM structure of the Arabidopsisthaliana ribosome in translating and non-translating states.

Structure (London, England : 1993)·2026
See all related articles

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Recognition

Background:

  • Protein domains are crucial for cellular functions.
  • Protein Tyrosine-Binding (PTB) domains and PSD-95/Discs-Large/ZO-1 (PDZ) domains are key protein interaction modules.
  • Understanding their structural and functional relationships is vital for deciphering complex biological pathways.

Purpose of the Study:

  • To investigate the structural and functional relationship between PTB domains and PDZ domains.
  • To identify conserved features and novel characteristics of these protein recognition motifs.

Main Methods:

  • Comparative structural analysis of PTB and PDZ domains.
  • Bioinformatic analysis of protein sequences and structures.
  • Literature review of known peptide-protein interactions mediated by these domains.

Related Experiment Videos

Main Results:

  • The PTB domain expands the known set of PH-domain interactions.
  • PTB domains function as peptide-protein recognition motifs.
  • The PDZ domain displays an intriguing structural resemblance to PTB domains.

Conclusions:

  • PTB domains represent a significant expansion in the understanding of PH-domain interactions.
  • The observed resemblance between PTB and PDZ domains suggests potential shared evolutionary origins or convergent functional adaptations.
  • Further research into these similarities could uncover novel therapeutic targets for diseases involving protein-protein interactions.