Publication Abstract from PubMed
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 3(10)-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 3(10)-helix.
Solution structure of the region 51-160 of human KIN17 reveals an atypical winged helix domain.,Carlier L, Couprie J, le Maire A, Guilhaudis L, Milazzo-Segalas I, Courcon M, Moutiez M, Gondry M, Davoust D, Gilquin B, Zinn-Justin S Protein Sci. 2007 Dec;16(12):2750-5. PMID:18029424[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
