Article
Structural characterization of filaments formed by human Xrcc4-Cernunnos/XLF complex involved in nonhomologous DNA end-joining.
Proceedings of the National Academy of Sciences of the United States of America - 2 Aug 2011
Ropars Virginie, Drevet Pascal, Legrand Pierre, Baconnais Sonia, Amram Jeremy, Faure Guilhem, Márquez José A, Piétrement Olivier, Guerois Raphaël, Callebaut Isabelle, Le Cam Eric, Revy Patrick, de Villartay Jean-Pierre, Charbonnier Jean-Baptiste
Abstract excerpt
Cernunnos/XLF is a core protein of the nonhomologous DNA end-joining (NHEJ) pathway that processes the majority of DNA double-strand breaks in mammals. Cernunnos stimulates the final ligation step catalyzed by the complex between DNA ligase IV and Xrcc4 (X4). Here we present the crystal structure of the X4(1-157)-Cernunnos(1-224) complex at 5.5-Å resolution and identify the relative positions of the two factors...
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