4CRI
Crystal Structure of 53BP1 tandem tudor domains in complex with methylated K810 Rb peptide
Summary for 4CRI
| Entry DOI | 10.2210/pdb4cri/pdb |
| Descriptor | TUMOR SUPPRESSOR P53-BINDING PROTEIN 1, RB1 PROTEIN (3 entities in total) |
| Functional Keywords | peptide binding protein, tumour suppressor prb, 53bp1 |
| Biological source | HOMO SAPIENS (HUMAN) More |
| Cellular location | Nucleus: Q12888 |
| Total number of polymer chains | 4 |
| Total formula weight | 42778.12 |
| Authors | Krojer, T.,Johansson, C.,Gileadi, C.,Fedorov, O.,Carr, S.,La Thangue, N.B.,Vollmar, M.,Crawley, L.,von Delft, F.,Bountra, C.,Arrowsmith, C.H.,Edwards, A.,Oppermann, U. (deposition date: 2014-02-26, release date: 2014-08-06, Last modification date: 2023-12-20) |
| Primary citation | Carr, S.M.,Munro, S.,Zalmas, L.,Fedorov, O.,Johansson, C.,Krojer, T.,Sagum, C.A.,Bedford, M.T.,Oppermann, U.,La Thangue, N.B. Lysine Methylation-Dependent Binding of 53BP1 to the Prb Tumor Suppressor. Proc.Natl.Acad.Sci.USA, 111:11341-, 2014 Cited by PubMed Abstract: The retinoblastoma tumor suppressor protein pRb is a key regulator of cell cycle progression and mediator of the DNA damage response. Lysine methylation at K810, which occurs within a critical Cdk phosphorylation motif, holds pRb in the hypophosphorylated growth-suppressing state. We show here that methyl K810 is read by the tandem tudor domain containing tumor protein p53 binding protein 1 (53BP1). Structural elucidation of 53BP1 in complex with a methylated K810 pRb peptide emphasized the role of the 53BP1 tandem tudor domain in recognition of the methylated lysine and surrounding residues. Significantly, binding of 53BP1 to methyl K810 occurs on E2 promoter binding factor target genes and allows pRb activity to be effectively integrated with the DNA damage response. Our results widen the repertoire of cellular targets for 53BP1 and suggest a previously unidentified role for 53BP1 in regulating pRb tumor suppressor activity. PubMed: 25049398DOI: 10.1073/PNAS.1403737111 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.35 Å) |
Structure validation
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