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3bqo

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3bqo, resolution 2.00Å ()
Gene: TERF1, PIN2, TRBF1, TRF, TRF1 (Homo sapiens), TINF2, TIN2 (Homo sapiens)
Domains: TRFH
Related: 3bu8, 3bua
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of TRF1 TRFH domain and TIN2 peptide complex

Publication Abstract from PubMed

Mammalian telomeres are protected by a six-protein complex, shelterin. Shelterin contains two closely related proteins, TRF1 and TRF2, which recruit various proteins to telomeres. Here we dissect the interactions of TRF1 and TRF2 with their shared binding partner, TIN2, and other shelterin accessory factors. TRF1 recognizes TIN2 using a conserved molecular surface in its TRF homology (TRFH) domain. However, this same surface does not act as a TIN2 binding site in TRF2, and TIN2 binding to TRF2 is mediated by a region outside the TRFH domain. Instead, the TRFH docking site of TRF2 binds a shelterin accessory factor Apollo, which does not interact with the TRFH domain of TRF1. Conversely, the TRFH domain of TRF1, but not of TRF2, interacts with another shelterin associated factor PinX1.

A Shared Docking Motif in TRF1 and TRF2 Used for Differential Recruitment of Telomeric Proteins., Chen Y, Yang Y, van Overbeek M, Donigian JR, Baciu P, de Lange T, Lei M, Science. 2008 Jan 17;. PMID:18202258

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

3BQO is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Chen Y, Yang Y, van Overbeek M, Donigian JR, Baciu P, de Lange T, Lei M. A Shared Docking Motif in TRF1 and TRF2 Used for Differential Recruitment of Telomeric Proteins. Science. 2008 Jan 17;. PMID:18202258

Page seeded by OCA on Tue Feb 17 04:53:04 2009

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