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Related Experiment Videos

Redox-regulated conformational changes in an SH3 domain.

Jürgen Zimmermann1, Ronald Kühne, Marc Sylvester

  • 1Protein Engineering Group, Leibniz-Institut für Molekulare Pharmakologie und Freie Universität Berlin, 13125 Berlin, Germany.

Biochemistry
|May 22, 2007
PubMed
Summary
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Cellular redox sensing involves reversible disulfide bonds in protein domains. This study reveals oxidation in the ADAP hSH3N domain alters its structure, impacting T cell activation signaling.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Structural Biology

Background:

  • Proteins undergo oxidation-induced conformational changes to sense cellular redox states.
  • Regulatory redox events require specific and transient protein modifications, unlike irreversible oxidative stress damage.

Purpose of the Study:

  • To investigate the reversible formation of a vicinal disulfide bond in a protein interaction domain.
  • To elucidate the structural consequences of this oxidation in the N-terminal hSH3 domain (hSH3N) of ADAP.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy was employed to determine the structure of the hSH3N domain.
  • Structural analysis was performed on both reduced and oxidized states of the protein.

Main Results:

Related Experiment Videos

  • A reversible, eight-membered ring formed via a vicinal disulfide bond between neighboring cysteines upon oxidation.
  • This oxidation induced significant conformational changes in the arginine-threonine (RT) loop and altered helix-sheet packing within the hSH3N domain.
  • The redox potential for this structural transition was determined to be -228 mV at pH 7.4.

Conclusions:

  • The reversible disulfide bond formation in the hSH3N domain is a specific redox-sensitive mechanism.
  • The observed structural changes and redox potential are consistent with a role in redox signaling during T cell activation.