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Related Experiment Video

Updated: Jul 5, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

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Published on: May 13, 2020

The crystal structure and dimerization interface of GADD45gamma.

Joseph D Schrag¹, Sarn Jiralerspong, Myriam Banville

¹Biotechnology Research Institute, National Research Council Canada, 6100 Royalmount Avenue, Montreal, QC, Canada. joe.schrag@nrc-cnrc.gc.ca

Proceedings of the National Academy of Sciences of the United States of America

|May 1, 2008

Summary

Growth arrest protein Gadd45gamma forms dimers essential for its tumor suppressor function. Understanding its structure reveals how protein interactions regulate Gadd45 family functions, impacting cell cycle control and apoptosis.

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Iterative Optimization of DNA Duplexes for Crystallization of SeqA-DNA Complexes

Iterative Optimization of DNA Duplexes for Crystallization of SeqA-DNA Complexes

Published on: November 1, 2012

Area of Science:

Molecular Biology
Structural Biology
Biochemistry

Background:

Gadd45 proteins function as tumor and autoimmune suppressors, with expression induced by genotoxic stress.
These proteins play roles in cell cycle control, growth arrest, and apoptosis via diverse protein interactions.

Purpose of the Study:

To determine the crystal structure of Gadd45gamma.
To investigate the role of Gadd45gamma dimerization in its biological functions.

Main Methods:

X-ray crystallography was used to determine the Gadd45gamma structure.
Point mutations were generated to disrupt the identified dimer interface.
Cell-based assays were performed to assess the functional impact of dimerization disruption.

Main Results:

The crystal structure of Gadd45gamma revealed an alphabetaalpha sandwich fold.
A dimer interface involving a four-helix bundle, utilizing highly conserved residues, was identified.
Disruption of dimerization through point mutations abolished Gadd45gamma's growth inhibitory function.

Conclusions:

Gadd45gamma forms dimers through a conserved interface.
Dimerization is critical for Gadd45gamma's role in growth inhibition.
Structural insights provide a framework for understanding Gadd45 family protein interactions and functions.