1H6O
Dimerisation domain from human TRF1
Summary for 1H6O
| Entry DOI | 10.2210/pdb1h6o/pdb |
| Related | 1BA5 |
| Descriptor | TELOMERIC REPEAT BINDING FACTOR 1 (1 entity in total) |
| Functional Keywords | telomere binding, trf1, telomere, dimerisation, trfh, dna-binding, nuclear protein |
| Biological source | HOMO SAPIENS (HUMAN) |
| Total number of polymer chains | 1 |
| Total formula weight | 23326.76 |
| Authors | Fairall, L.,Chapman, L.,Rhodes, D. (deposition date: 2001-06-20, release date: 2001-09-05, Last modification date: 2024-04-24) |
| Primary citation | Fairall, L.,Chapman, L.,Moss, H.,de Lange, T.,Rhodes, D. Structure of the TRFH dimerization domain of the human telomeric proteins TRF1 and TRF2. Mol.Cell, 8:351-361, 2001 Cited by PubMed Abstract: TRF1 and TRF2 are key components of vertebrate telomeres. They bind to double-stranded telomeric DNA as homodimers. Dimerization involves the TRF homology (TRFH) domain, which also mediates interactions with other telomeric proteins. The crystal structures of the dimerization domains from human TRF1 and TRF2 were determined at 2.9 and 2.2 A resolution, respectively. Despite a modest sequence identity, the two TRFH domains have the same entirely alpha-helical architecture, resembling a twisted horseshoe. The dimerization interfaces feature unique interactions that prevent heterodimerization. Mutational analysis of TRF1 corroborates the structural data and underscores the importance of the TRFH domain in dimerization, DNA binding, and telomere localization. A possible structural homology between the TRFH domain of fission yeast telomeric protein Taz1 with those of the vertebrate TRFs is suggested. PubMed: 11545737DOI: 10.1016/s1097-2765(01)00321-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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