1ssf

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1ssf

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Solution structure of the mouse 53BP1 fragment (residues 1463-1617)

Overview

53BP1 is a key transducer of the DNA damage checkpoint signal, which is, required for phosphorylation of a subset of ATM substrates and p53, accumulation. After cell irradiation, the 53BP1 N-terminal region is, phosphorylated. Its two C-terminal BRCT motifs interact with p53. Its, central region is required and sufficient for 53BP1 foci formation at DNA, strand breaks and for 53BP1 binding to the kinetochore. It contains an, RG-rich segment and interacts with DNA in vitro. Here we show that the, major globular domain of the 53BP1 central region adopts a new structural, motif composed of two tightly packed Tudor domains and a C-terminal alpha, helix. A unique surface essentially located on the first Tudor domain is, involved in the binding to 53BP1 RG-rich sequence and to DNA, suggesting, that the Tudor tandem can act as an adaptor mediating intramolecular as, well as intermolecular protein-protein interactions and protein-nucleic, acid associations.

About this Structure

1SSF is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

The Tudor tandem of 53BP1: a new structural motif involved in DNA and RG-rich peptide binding., Charier G, Couprie J, Alpha-Bazin B, Meyer V, Quemeneur E, Guerois R, Callebaut I, Gilquin B, Zinn-Justin S, Structure. 2004 Sep;12(9):1551-62. PMID:15341721

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