1h6p

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spinqualitylabelsall models PDB ID 1h6p Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
, resolution 2.20Å
Ligands:
Coordinates:	save as pdb, mmCIF, xml

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. 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

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