Structural basis for recognition of 53BP1 tandem Tudor domain by TIRR

Yaxin Dai; Aili Zhang; Shan Shan; Zihua Gong; Zheng Zhou

doi:10.1038/s41467-018-04557-2

Nature Communications (May 2018)

Structural basis for recognition of 53BP1 tandem Tudor domain by TIRR

Yaxin Dai,
Aili Zhang,
Shan Shan,
Zihua Gong,
Zheng Zhou

Affiliations

Yaxin Dai: National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences
Aili Zhang: Department of Cancer Biology, Cleveland Clinic Lerner Research Institute
Shan Shan: National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences
Zihua Gong: Department of Cancer Biology, Cleveland Clinic Lerner Research Institute
Zheng Zhou: National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences

DOI: https://doi.org/10.1038/s41467-018-04557-2
Journal volume & issue: Vol. 9, no. 1
pp. 1 – 12

Abstract

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The p53-binding protein 1 (53BP1) regulates the choice of the DNA double-strand break repair pathway. Here the authors present the crystal structure of Tudor-interacting repair regulator (TIRR) bound to the 53BP1 tandem Tudor domain, which reveals how TIRR blocks H4K20me2 binding to 53BP1 Tudor and functionally differs from its paralog Nudt16.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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