3BU8

Crystal Structure of TRF2 TRFH domain and TIN2 peptide complex

Summary for 3BU8

• Entry DOI: 10.2210/pdb3bu8/pdb
• Related: 3BQO 3BUA
• Descriptor: Telomeric repeat-binding factor 2, TERF1-interacting nuclear factor 2 (3 entities in total)
• Functional Keywords: trf2 trfh domain trf2 dimerization domain tin2 peptide, alternative splicing, cell cycle, chromosomal protein, dna-binding, nucleus, phosphoprotein, telomere, dna binding protein
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: Q15554; Nucleus. Isoform 1: Nucleus matrix: Q9BSI4
• Total number of polymer chains: 4
• Total formula weight: 58269.28

Authors

Chen, Y.,Yang, Y.,van Overbeek, M.,Donigian, J.R.,Baciu, P.,de Lange, T.,Lei, M. (deposition date: 2008-01-02, release date: 2008-02-19, Last modification date: 2023-08-30)

Primary citation

Chen, Y.,Yang, Y.,van Overbeek, M.,Donigian, J.R.,Baciu, P.,de Lange, T.,Lei, M.
A shared docking motif in TRF1 and TRF2 used for differential recruitment of telomeric proteins.
Science, 319:1092-1096, 2008

PubMed Abstract: Mammalian telomeres are protected by a six-protein complex: shelterin. Shelterin contains two closely related proteins (TRF1 and TRF2), which recruit various proteins to telomeres. We dissect the interactions of TRF1 and TRF2 with their shared binding partner (TIN2) and other shelterin accessory factors. TRF1 recognizes TIN2 using a conserved molecular surface in its TRF homology (TRFH) domain. However, this same surface does not act as a TIN2 binding site in TRF2, and TIN2 binding to TRF2 is mediated by a region outside the TRFH domain. Instead, the TRFH docking site of TRF2 binds a shelterin accessory factor (Apollo), which does not interact with the TRFH domain of TRF1. Conversely, the TRFH domain of TRF1, but not of TRF2, interacts with another shelterin-associated factor: PinX1.

PubMed: 18202258
DOI: 10.1126/science.1151804

Experimental method

X-RAY DIFFRACTION (2.15 Å)