1h6p
From Proteopedia
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DIMERISTION DOMAIN FROM HUMAN TRF2
Overview
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.
About this Structure
1H6P is a Single protein structure of sequence from Homo sapiens with MG as ligand. Full crystallographic information is available from OCA.
Reference
Structure of the TRFH dimerization domain of the human telomeric proteins TRF1 and TRF2., Fairall L, Chapman L, Moss H, de Lange T, Rhodes D, Mol Cell. 2001 Aug;8(2):351-61. PMID:11545737
Page seeded by OCA on Mon Nov 12 17:13:32 2007
Categories: Homo sapiens | Single protein | Chapman, L. | Fairall, L. | Rhodes, D. | MG | Dimerisation | Dna-binding | Nuclear protein | Telomere | Trf2 | Trfh
