1BA5
DNA-BINDING DOMAIN OF HUMAN TELOMERIC PROTEIN, HTRF1, NMR, 18 STRUCTURES
Summary for 1BA5
| Entry DOI | 10.2210/pdb1ba5/pdb |
| NMR Information | BMRB: 4210 |
| Descriptor | HTRF1 (1 entity in total) |
| Functional Keywords | dna-binding domain, myb repeats, telomeres, trf |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: P54274 |
| Total number of polymer chains | 1 |
| Total formula weight | 6668.81 |
| Authors | Nishikawa, T.,Nagadoi, A.,Yoshimura, S.,Aimoto, S.,Nishimura, Y. (deposition date: 1998-04-22, release date: 1999-04-27, Last modification date: 2024-05-22) |
| Primary citation | Nishikawa, T.,Nagadoi, A.,Yoshimura, S.,Aimoto, S.,Nishimura, Y. Solution structure of the DNA-binding domain of human telomeric protein, hTRF1. Structure, 6:1057-1065, 1998 Cited by PubMed Abstract: Mammalian telomeres consist of long tandem arrays of the double-stranded TTAGGG sequence motif packaged by a telomere repeat binding factor, TRF1. The DNA-binding domain of TRF1 shows sequence homology to each of three tandem repeats of the DNA-binding domain of the transcriptional activator c-Myb. The isolated c-Myb-like domain of human TRF1 (hTRF1) binds specifically to telomeric DNA as a monomer, in a similar manner to that of homeodomains. So far, the only three-dimensional structure of a telomeric protein to be determined is that of a yeast telomeric protein, Rap 1p. The DNA-binding domain of Rap 1p contains two subdomains that are structurally closely related to c-Myb repeats. We set out to determine the solution structure of the DNA-binding domain of hTRF1 in order to establish its mode of DNA binding. PubMed: 9739097DOI: 10.1016/S0969-2126(98)00106-3 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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