6HM4
Crystal structure of Rad4 BRCT1,2 in complex with a Mdb1 phosphopeptide
Summary for 6HM4
| Entry DOI | 10.2210/pdb6hm4/pdb |
| Descriptor | S-M checkpoint control protein rad4, DNA damage response protein Mdb1, ACETATE ION, ... (5 entities in total) |
| Functional Keywords | brct domain phosphopeptide recognition, cell cycle |
| Biological source | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) More |
| Total number of polymer chains | 2 |
| Total formula weight | 23112.44 |
| Authors | Day, M.,Rappas, M.,Oliver, A.W.,Pearl, L.H. (deposition date: 2018-09-12, release date: 2018-10-17, Last modification date: 2024-11-20) |
| Primary citation | Day, M.,Rappas, M.,Ptasinska, K.,Boos, D.,Oliver, A.W.,Pearl, L.H. BRCT domains of the DNA damage checkpoint proteins TOPBP1/Rad4 display distinct specificities for phosphopeptide ligands. Elife, 7:-, 2018 Cited by PubMed Abstract: TOPBP1 and its fission yeast homologueRad4, are critical players in a range of DNA replication, repair and damage signalling processes. They are composed of multiple BRCT domains, some of which bind phosphorylated motifs in other proteins. They thus act as multi-point adaptors bringing proteins together into functional combinations, dependent on post-translational modifications downstream of cell cycle and DNA damage signals. We have now structurally and/or biochemically characterised a sufficient number of high-affinity complexes for the conserved N-terminal region of TOPBP1 and Rad4 with diverse phospho-ligands, including human RAD9 and Treslin, and Crb2 and Sld3, to define the determinants of BRCT domain specificity. We use this to identify and characterise previously unknown phosphorylation-dependent TOPBP1/Rad4-binding motifs in human RHNO1 and the fission yeast homologue of MDC1, Mdb1. These results provide important insights into how multiple BRCT domains within TOPBP1/Rad4 achieve selective and combinatorial binding of their multiple partner proteins. PubMed: 30295604DOI: 10.7554/eLife.39979 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.77018592355 Å) |
Structure validation
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