2V1N

SOLUTION STRUCTURE OF THE REGION 51-160 OF HUMAN KIN17 REVEALS A WINGED HELIX FOLD

Summary for 2V1N

• Entry DOI: 10.2210/pdb2v1n/pdb
• Related: 2CKK
• NMR Information: BMRB: 6938
• Descriptor: PROTEIN KIN HOMOLOG (1 entity in total)
• Functional Keywords: kin17, nuclear protein, winged helix motif
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 1
• Total formula weight: 13686.45

Authors

Carlier, L.,Le Maire, A.,Gondry, M.,Guilhaudis, L.,Milazzo, I.,Davoust, D.,Couprie, J.,Gilquin, B.,Zinn-Justin, S. (deposition date: 2007-05-27, release date: 2007-11-27, Last modification date: 2024-05-15)

Primary citation

Carlier, L.,Le Maire, A.,Gondry, M.,Guilhaudis, L.,Milazzo, I.,Davoust, D.,Couprie, J.,Gilquin, B.,Zinn-Justin, S.
Solution Structure of the Region 51-160 of Human Kin17 Reveals an Atypical Winged Helix Domain
Protein Sci., 16:2750-, 2007

PubMed 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.

PubMed: 18029424
DOI: 10.1110/PS.073079107

Experimental method

SOLUTION NMR