3OLC

Crystal structure of the N-terminal region of TopBP1

Summary for 3OLC

• Entry DOI: 10.2210/pdb3olc/pdb
• Descriptor: DNA topoisomerase 2-binding protein 1 (2 entities in total)
• Functional Keywords: brct domain, dna repair, rad9, dna binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q92547
• Total number of polymer chains: 1
• Total formula weight: 35230.43

Authors

Huo, Y.G.,Bai, L.,Xu, M.,Jiang, T. (deposition date: 2010-08-25, release date: 2011-03-30, Last modification date: 2024-11-20)

Primary citation

Huo, Y.G.,Bai, L.,Xu, M.,Jiang, T.
Crystal structure of the N-terminal region of human Topoisomerase II beta binding protein 1
Biochem.Biophys.Res.Commun., 401:401-405, 2010

PubMed Abstract: Human DNA Topoisomerase IIβ binding protein 1 (TopBP1) is a modulating protein that plays an essential role in the response to DNA damage. The N-terminal region of TopBP1, which contains predicted BRCA1-carboxy terminal (BRCT) domains 1 and 2, binds to Rad9, a component of the cell cycle checkpoint clamp Rad9-Hus1-Rad1 complex. Here, we report the crystal structure of the TopBP1N-terminal region (residues 1-290) at 2.4Å resolution. Interestingly, in addition to the predicted tandem BRCT1-2 repeats (residues 103-284), residues 7-98 form a previously unreported BRCT domain (here, BRCT0). In contrast to both BRCT1 and BRCT2, which possess the conventional phosphopeptide binding residues within a surface pocket, the corresponding pocket in BRCT0 is largely hydrophobic. Structural comparisons together with peptide binding studies indicate that the tandem BRCT1-2 domains are the binding region for phosphorylated Ser387 in Rad9.

PubMed: 20858457
DOI: 10.1016/j.bbrc.2010.09.066

Experimental method

X-RAY DIFFRACTION (2.4 Å)