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Structure of the TRFH dimerization domain of the human telomeric proteins TRF1 and TRF2.
- Source :
-
Molecular cell [Mol Cell] 2001 Aug; Vol. 8 (2), pp. 351-61. - Publication Year :
- 2001
-
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.
- Subjects :
- Amino Acid Sequence
Crystallography, X-Ray
DNA-Binding Proteins genetics
Dimerization
Fungal Proteins genetics
Humans
Models, Molecular
Molecular Sequence Data
Mutagenesis, Site-Directed
Nuclear Proteins chemistry
Protein Binding
RNA-Binding Proteins chemistry
Sequence Alignment
Telomere chemistry
Telomeric Repeat Binding Protein 1
Telomeric Repeat Binding Protein 2
DNA-Binding Proteins chemistry
Protein Structure, Tertiary
Schizosaccharomyces pombe Proteins
Telomere-Binding Proteins
Subjects
Details
- Language :
- English
- ISSN :
- 1097-2765
- Volume :
- 8
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Molecular cell
- Publication Type :
- Academic Journal
- Accession number :
- 11545737
- Full Text :
- https://doi.org/10.1016/s1097-2765(01)00321-5