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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, Courçon M, Moutiez M, Gondry M, Davoust D, Gilquin B, Zinn-Justin S
Protein Sci 16 2750-5 (2007)
Cited: 12 times
EuropePMC logo PMID: 18029424

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.

Articles - 2v1n mentioned but not cited (3)

  1. 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, Courçon M, Moutiez M, Gondry M, Davoust D, Gilquin B, Zinn-Justin S. Protein Sci. 16 2750-2755 (2007)
  2. The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins. Chakraborty S, Rendón-Ramírez A, Ásgeirsson B, Dutta M, Ghosh AS, Oda M, Venkatramani R, Rao BJ, Dandekar AM, Goñi FM. F1000Res 2 286 (2013)
  3. A genetic screen in C. elegans reveals roles for KIN17 and PRCC in maintaining 5' splice site identity. Suzuki JMNGL, Osterhoudt K, Cartwright-Acar CH, Gomez DR, Katzman S, Zahler AM. PLoS Genet 18 e1010028 (2022)


Reviews citing this publication (1)

  1. Roles and regulatory mechanisms of KIN17 in cancers (Review). Huang X, Dai Z, Li Q, Lin X, Huang Q, Zeng T. Oncol Lett 25 137 (2023)

Articles citing this publication (8)

  1. Structural and Functional Insights into Human Re-initiation Complexes. Weisser M, Schäfer T, Leibundgut M, Böhringer D, Aylett CHS, Ban N. Mol. Cell 67 447-456.e7 (2017)
  2. Methylation of the DNA/RNA-binding protein Kin17 by METTL22 affects its association with chromatin. Cloutier P, Lavallée-Adam M, Faubert D, Blanchette M, Coulombe B. J Proteomics 100 115-124 (2014)
  3. Purification and structural study of the voltage-sensor domain of the human KCNQ1 potassium ion channel. Peng D, Kim JH, Kroncke BM, Law CL, Xia Y, Droege KD, Van Horn WD, Vanoye CG, Sanders CR. Biochemistry 53 2032-2042 (2014)
  4. 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. Garcia-Molina A, Xing S, Huijser P. Plant Physiol. 164 828-840 (2014)
  5. Structure of the frequency-interacting RNA helicase: a protein interaction hub for the circadian clock. Conrad KS, Hurley JM, Widom J, Ringelberg CS, Loros JJ, Dunlap JC, Crane BR. EMBO J. 35 1707-1719 (2016)
  6. Biophysical characterization and molecular phylogeny of human KIN protein. Pattaro Júnior JR, Caruso ÍP, de Lima Neto QA, Duarte Junior FF, Dos Santos Rando F, Gerhardt ECM, Fernandez MA, Seixas FAV. Eur Biophys J 48 645-657 (2019)
  7. Interactome Analysis of KIN (Kin17) Shows New Functions of This Protein. Gaspar VP, Ramos AC, Cloutier P, Pattaro Junior JR, Duarte Junior FF, Bouchard A, Seixas FAV, Coulombe B, Fernandez MA. Curr Issues Mol Biol 43 767-781 (2021)
  8. The Arabidopsis KIN17 and its homolog KLP mediate different aspects of plant growth and development. Garcia-Molina A, Xing S, Huijser P. Plant Signal Behav 9 e28634 (2014)


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