1SSF

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

Summary for 1SSF

• Entry DOI: 10.2210/pdb1ssf/pdb
• NMR Information: BMRB: 5878
• Descriptor: Transformation related protein 53 binding protein 1 (1 entity in total)
• Functional Keywords: tudor domains, tandem, sh3-like fold, beta barrel, alpha-helix, cell cycle
• Biological source: Mus musculus (house mouse)
• Total number of polymer chains: 1
• Total formula weight: 17426.57

Authors

Charier, G.,Couprie, J.,Alpha-Bazin, B.,Meyer, V.,Quemeneur, E.,Guerois, R.,Callebaut, I.,Gilquin, B.,Zinn-Justin, S. (deposition date: 2004-03-24, release date: 2004-09-14, Last modification date: 2024-05-22)

Primary citation

Charier, G.,Couprie, J.,Alpha-Bazin, B.,Meyer, V.,Quemeneur, E.,Guerois, R.,Callebaut, I.,Gilquin, B.,Zinn-Justin, S.
The Tudor Tandem of 53BP1; A New Structural Motif Involved in DNA and RG-Rich Peptide Binding
Structure, 12:1551-1562, 2004

PubMed Abstract: 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.

PubMed: 15341721
DOI: 10.1016/j.str.2004.06.014

Experimental method

SOLUTION NMR