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Protein Science (2007), 16:2750-2755. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society
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PROTEIN STRUCTURE REPORT

Solution structure of the region 51–160 of human KIN17 reveals an atypical winged helix domain

Ludovic Carlier1, Joël Couprie2, Albane le Maire2, Laure Guilhaudis1, Isabelle Milazzo-Segalas1, Marie Courçon2, Mireille Moutiez2, Muriel Gondry2, Daniel Davoust1, Bernard Gilquin2, and Sophie Zinn-Justin2

1 Equipe de Chimie Organique et Biologie Structurale, IFRMP 23, CNRS UMR 6014, Université de Rouen, 76821 Mont-Saint-Aignan, France
2 CEA de Saclay, Institut de Biologie et Technologies iBiTec-S, 91190 Gif-sur-Yvette, France

(RECEIVED June 21, 2007; FINAL REVISION August 22, 2007; ACCEPTED September 20, 2007)

Human KIN17 is a 45-kDa eukaryotic DNA- and RNA-binding protein that plays an important role in nuclear metabolism and in particular in the general response to genotoxics. Its amino acids sequence contains a zinc finger motif (residues 28–50) within a 30-kDa N-terminal region conserved from yeast to human, and a 15-kDa C-terminal tandem of SH3-like subdomains (residues 268–393) only found in higher eukaryotes. Here we report the solution structure of the region 51–160 of human KIN17. We show that this fragment folds into a three-{alpha}-helix bundle packed against a three-stranded beta-sheet. It belongs to the winged helix (WH) family. Structural comparison with analogous WH domains reveals that KIN17 WH module presents an additional and highly conserved 310-helix. Moreover, KIN17 WH helix H3 is not positively charged as in classical DNA-binding WH domains. Thus, human KIN17 region 51–160 might rather be involved in protein–protein interaction through its conserved surface centered on the 310-helix.

Keywords: KIN17 protein; winged helix fold; NMR structure; nuclear metabolism


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