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5XUP

Crystal structure of TRF1 and TERB1

Summary for 5XUP
Entry DOI10.2210/pdb5xup/pdb
DescriptorTelomeric repeat-binding factor 1, Telomere repeats-binding bouquet formation protein 1 (3 entities in total)
Functional Keywordstelomere, meiosis, dna binding protein
Biological sourceHomo sapiens (Human)
More
Cellular locationNucleus: P54274
Chromosome, telomere : Q8NA31
Total number of polymer chains4
Total formula weight49307.02
Authors
Long, J.,Huang, C.,Wu, J.,Lei, M. (deposition date: 2017-06-24, release date: 2017-11-01, Last modification date: 2023-11-22)
Primary citationLong, 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: 29083416
DOI: 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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