ArticleProtein science : a publication of the Protein Society2007
Solution structure of the region 51-160 of human KIN17 reveals an atypical winged helix domain.
Article in Protein science : a publication of the Protein Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 20 citations in OpenAlex.
- Roles and regulatory mechanisms of KIN17 in cancers (Review).Oncology letters · 2023Review
- A genetic screen in C. elegans reveals roles for KIN17 and PRCC in maintaining 5' splice site identity.PLoS genetics · 2022Article
- Interactome Analysis of KIN (Kin17) Shows New Functions of This Protein.Current issues in molecular biology · 2021Article
- Biophysical characterization and molecular phylogeny of human KIN protein.European biophysics journal : EBJ · 2019Article
- Structure of the frequency-interacting RNA helicase: a protein interaction hub for the circadian clock.The EMBO journal · 2016Article
- Purification and structural study of the voltage-sensor domain of the human KCNQ1 potassium ion channel.Biochemistry · 2014Article
- A conserved KIN17 curved DNA-binding domain protein assembles with SQUAMOSA PROMOTER-BINDING PROTEIN-LIKE7 to adapt Arabidopsis growth and development to limiting copper availability.Plant physiology · 2014Article
- The Arabidopsis KIN17 and its homolog KLP mediate different aspects of plant growth and development.Plant signaling & behavior · 2014Article
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Authors and funding
11 authors at 5 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
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.
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