5XUP
Crystal structure of TRF1 and TERB1
Summary for 5XUP
Entry DOI | 10.2210/pdb5xup/pdb |
Descriptor | Telomeric repeat-binding factor 1, Telomere repeats-binding bouquet formation protein 1 (3 entities in total) |
Functional Keywords | telomere, meiosis, dna binding protein |
Biological source | Homo sapiens (Human) More |
Cellular location | Nucleus: P54274 Chromosome, telomere : Q8NA31 |
Total number of polymer chains | 4 |
Total formula weight | 49307.02 |
Authors | |
Primary citation | Long, J.,Huang, C.,Chen, Y.,Zhang, Y.,Shi, S.,Wu, L.,Liu, Y.,Liu, C.,Wu, J.,Lei, M. Telomeric TERB1-TRF1 interaction is crucial for male meiosis. Nat. Struct. Mol. Biol., 24:1073-1080, 2017 Cited by PubMed Abstract: During meiotic prophase, the meiosis-specific telomere-binding protein TERB1 regulates chromosome movement required for homologous pairing and recombination by interacting with the telomeric shelterin subunit TRF1. Here, we report the crystal structure of the TRF1-binding motif of human TERB1 in complex with the TRFH domain of TRF1. Notably, specific disruption of the TERB1-TRF1 interaction by a point mutation in the mouse Terb1 gene results in infertility only in males. We find that this mutation causes an arrest in the zygotene-early pachytene stage and mild telomere abnormalities of autosomes but unpaired X and Y chromosomes in pachytene, leading to massive spermatocyte apoptosis. We propose that the loss of telomere structure mediated by the TERB1-TRF1 interaction significantly affects homologous pairing of the telomere-adjacent pseudoautosomal region (PAR) of the X and Y chromosomes in mouse spermatocytes. Our findings uncover a specific mechanism of telomeres that surmounts the unique challenges of mammalian X-Y pairing in meiosis. PubMed: 29083416DOI: 10.1038/nsmb.3496 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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