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Structure paper

TitleA shared docking motif in TRF1 and TRF2 used for differential recruitment of telomeric proteins.
Journal, issue, pagesScience, Vol. 319, Page 1092-1096, Year 2008
Publish dateDec 20, 2007 (structure data deposition date)
AuthorsChen, Y. / Yang, Y. / van Overbeek, M. / Donigian, J.R. / Baciu, P. / de Lange, T. / Lei, M.
External linksScience / PubMed:18202258
MethodsX-ray diffraction
Resolution2 - 2.5 Å
Structure data

PDB-3bqo:
Crystal Structure of TRF1 TRFH domain and TIN2 peptide complex
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-3bu8:
Crystal Structure of TRF2 TRFH domain and TIN2 peptide complex
Method: X-RAY DIFFRACTION / Resolution: 2.15 Å

PDB-3bua:
Crystal Structure of TRF2 TRFH domain and APOLLO peptide complex
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsDNA BINDING PROTEIN / TRF1 TRFH domain Dimerization domain TIN2 / ADP-ribosylation / Alternative splicing / Cell cycle / Cell division / Chromosomal protein / DNA-binding / Mitosis / Nucleus / Phosphoprotein / Telomere / TRF2 TRFH domain TRF2 dimerization domain TIN2 peptide / TRF2 TRFH domain Dimerization domain APOLLO peptide / DNA damage / DNA repair / Polymorphism

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