NMR studies of telomeric nucleoprotein complexes involving the Myb-like domain of the human telomeric protein TRF2

Abstract : In order to study the binding of the Myb-like domain of the human telomeric protein TRF2 (Myb-TRF2) with different structural components of the t-loop model, we report NMR studies of the binding of Myb-TRF2 protein with two repeats human telomeric DNA under three conformations. Our results showed that Myb-TRF2 binds to the duplex and even to the quadruplex and the random coil G-rich strand. The solution structure of Myb-TRF2 reported here looks like Myb-TRF1 suggesting similar DNA binding mode. As a matter of fact, we have shown that its binding to the human telomeric duplex presents great similarities with this of Myb-TRF1.
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https://hal.archives-ouvertes.fr/hal-00088835
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Submitted on : Monday, August 7, 2006 - 11:39:37 AM
Last modification on : Thursday, May 9, 2019 - 4:02:04 PM

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Y. Bilbille, F. Paquet, H. Meudal, M.J. Giraud-Panis, G. Lancelot. NMR studies of telomeric nucleoprotein complexes involving the Myb-like domain of the human telomeric protein TRF2. Comptes Rendus Chimie, Elsevier Masson, 2006, 9 (3-4), pp.452-458. ⟨10.1016/j.crci.2005.06.019⟩. ⟨hal-00088835⟩

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