3JVE

Crystal Structure of the Sixth BRCT Domain of TopBP1

Summary for 3JVE

• Entry DOI: 10.2210/pdb3jve/pdb
• Descriptor: DNA topoisomerase 2-binding protein 1 (2 entities in total)
• Functional Keywords: brct domain, dna damage, dna repair, dna-binding, nucleus, phosphoprotein, polymorphism, ubl conjugation, dna binding protein, protein binding
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q92547
• Total number of polymer chains: 1
• Total formula weight: 12412.96

Authors

Leung, C.C.,Kellogg, E.,Baker, D.,Glover, J.N.M. (deposition date: 2009-09-16, release date: 2010-01-19, Last modification date: 2024-02-21)

Primary citation

Leung, C.C.,Kellogg, E.,Kuhnert, A.,Hanel, F.,Baker, D.,Glover, J.N.
Insights from the crystal structure of the sixth BRCT domain of topoisomerase IIbeta binding protein 1.
Protein Sci., 19:162-167, 2010

PubMed Abstract: Topoisomerase IIbeta binding protein 1 (TopBP1) is a major player in the DNA damage response and interacts with a number of protein partners via its eight BRCA1 carboxy-terminal (BRCT) domains. In particular, the sixth BRCT domain of TopBP1 has been implicated in binding to the phosphorylated transcription factor, E2F1, and poly(ADP-ribose) polymerase 1 (PARP-1), where the latter interaction is responsible for the poly(ADP-ribosyl)ation of TopBP1. To gain a better understanding of the nature of TopBP1 BRCT6 interactions, we solved the crystal structure of BRCT6 to 1.34 A. The crystal structure reveals a degenerate phospho-peptide binding pocket and lacks conserved hydrophobic residues involved in packing of tandem BRCT repeats, which, together with results from phospho-peptide binding studies, strongly suggest that TopBP1 BRCT6 independently does not function as a phospho-peptide binding domain. We further provide insight into poly(ADP-ribose) binding and sites of potential modification by PARP-1.

PubMed: 19937654
DOI: 10.1002/pro.290

Experimental method

X-RAY DIFFRACTION (1.34 Å)