|Title||SECONDARY STRUCTURE OF THE ETS DOMAIN PLACES MURINE ETS-1 IN THE SUPERFAMILY OF WINGED HELIX-TURN-HELIX DNA-BINDING PROTEINS|
|Publication Type||Journal Article|
|Year of Publication||1994|
|Authors||Donaldson, LW, Petersen, JM, Graves, BJ, McIntosh, LP|
|Type of Article||Article|
|Keywords||3-DIMENSIONAL NMR-SPECTROSCOPY, ASSIGNMENT, BACKBONE AMIDE, COUPLING-CONSTANTS, CRYSTAL-STRUCTURE, LARGER, MOTIF, PROTEINS, SIDE-CHAIN RESONANCES, SPECTRA, TRANSCRIPTION FACTORS|
The members of the ets gene family of transcription factors are characterized by a conserved 85-residue DNA-binding region, termed the ETS domain, that lacks sequence homology to structurally characterized DNA-binding motifs. The secondary structure of the ETS domain of murine Ets-1 was determined on the basis of NMR chemical shifts, NOE and J-coupling constraints, amide hydrogen exchange, circular dichroism, and FT-IR spectroscopy. The ETS domain is composed of three a-helices (H) and four beta-strands (S) arranged in the order H1-S1-S2-H2-H3-S3-S4. The four-stranded antiparallel beta-sheet is the scaffold for a putative helix-turn-helix DNA recognition motif formed by helices 2 and 3. The 25 residues extending beyond the ETS domain to the native C-terminus of the truncated Ets-1 also contain a helical segment. On the basis of the similarity of this topology with that of catabolite activator protein (CAP), heat shock factor (HSF), and hepatocyte nuclear factor (HNF-3 gamma), we propose that ets proteins are members of the superfamily of winged helix-turn-helix DNA-binding proteins.
|URL||<Go to ISI>://A1994PT48500001|