1GZH

Crystal structure of the BRCT domains of human 53BP1 bound to the p53 tumor supressor

Summary for 1GZH

• Entry DOI: 10.2210/pdb1gzh/pdb
• Related: 1A1U 1AIE 1DT7 1HS5 1KZY 1OLG 1OLH 1PES 1PET 1SAE 1SAF 1SAG 1SAH 1SAI 1SAJ 1SAK 1SAL 1TSR 1TUP 1YCQ 1YCS 3SAK
• Descriptor: CELLULAR TUMOR ANTIGEN P53, TUMOR SUPPRESSOR P53-BINDING PROTEIN 1, ZINC ION, ... (6 entities in total)
• Functional Keywords: gene regulation, anti-oncogene, dna-binding, transcription regulation, bcrt domain, apoptosis, disease mutation, activator, dna- repair
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Cytoplasm. Isoform 1: Nucleus. Isoform 2: Nucleus. Isoform 3: Nucleus. Isoform 4: Nucleus. Isoform 7: Nucleus. Isoform 8: Nucleus. Isoform 9: Cytoplasm: P04637 P04637; Nucleus: Q12888
• Total number of polymer chains: 4
• Total formula weight: 101411.68

Authors

Derbyshire, D.J.,Doherty, A.J. (deposition date: 2002-05-22, release date: 2002-06-27, Last modification date: 2023-12-13)

Primary citation

Derbyshire, D.J.,Basu, B.P.,Serpell, L.,Joo, W.,Date, T.,Iwabuchi, K.,Doherty, A.J.
Crystal Structure of Human 53BP1 Brct Domains Bound to P53 Tumour Suppressor
Embo J., 21:3863-, 2002

PubMed Abstract: The BRCT (BRCA1 C-terminus) is an evolutionary conserved protein-protein interacting module found as single, tandem or multiple repeats in a diverse range of proteins known to play roles in the DNA-damage response. The BRCT domains of 53BP1 bind to the tumour suppressor p53. To investigate the nature of this interaction, we have determined the crystal structure of the 53BP1 BRCT tandem repeat in complex with the DNA-binding domain of p53. The structure of the 53BP1-p53 complex shows that the BRCT tandem repeats pack together through a conserved interface that also involves the inter-domain linker. A comparison of the structure of the BRCT region of 53BP1 with the BRCA1 BRCT tandem repeat reveals that the interdomain interface and linker regions are remarkably well conserved. 53BP1 binds to p53 through contacts with the N-terminal BRCT repeat and the inter-BRCT linker. The p53 residues involved in this binding are mutated in cancer and are also important for DNA binding. We propose that BRCT domains bind to cellular target proteins through a conserved structural element termed the 'BRCT recognition motif'.

PubMed: 12110597
DOI: 10.1093/EMBOJ/CDF383

Experimental method

X-RAY DIFFRACTION (2.6 Å)