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

Protein phosphatases

D Barford1

  • 1University of Oxford, UK.

Current Opinion in Structural Biology
|December 1, 1995
PubMed
Summary

Protein phosphatases, which are crucial for cell signaling, have distinct structures and catalytic mechanisms. Analyzing their crystal structures offers insights into enzyme specificity and regulation.

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

Molecular mechanism of target RNA transcript recognition by Argonaute-guide complexes.

Cold Spring Harbor symposia on quantitative biology·2007
Same author

TYK2 and JAK2 are substrates of protein-tyrosine phosphatase 1B.

The Journal of biological chemistry·2001
Same author

The mechanism of protein kinase regulation by protein phosphatases.

Biochemical Society transactions·2001
Same author

Phosphoprotein-protein interactions revealed by the crystal structure of kinase-associated phosphatase in complex with phosphoCDK2.

Molecular cell·2001
Same author

Crystal structure of the M-fragment of alpha-catenin: implications for modulation of cell adhesion.

The EMBO journal·2001
Same author

Molecular basis for the dephosphorylation of the activation segment of the insulin receptor by protein tyrosine phosphatase 1B.

Molecular cell·2001

Area of Science:

  • Biochemistry
  • Enzymology
  • Structural Biology

Background:

  • Protein phosphatases are key signal-transducing enzymes.
  • They play critical roles in dephosphorylating cellular phosphoproteins.
  • Understanding their mechanisms is vital for cell signaling research.

Purpose of the Study:

  • To elucidate the structural and mechanistic differences between protein tyrosine and serine/threonine phosphatases.
  • To provide insights into substrate specificity and enzyme regulation based on structural data.

Main Methods:

  • X-ray crystallography was employed to determine the structures of protein tyrosine and serine/threonine phosphatases.
  • Comparative structural analysis was performed.

Main Results:

  • Protein tyrosine and serine/threonine phosphatases exhibit distinct three-dimensional structures.
  • These phosphatases utilize different enzymatic mechanisms for catalyzing dephosphorylation reactions.
  • Structural data revealed potential bases for substrate specificity.

Conclusions:

  • The distinct structures and mechanisms of protein phosphatases are key to their functions.
  • Crystal structures provide a foundation for understanding enzyme regulation and substrate specificity.

Related Experiment Videos