Open AccessSecondary structure of the lac repressor DNA-binding domain by two-dimensional 1H nuclear magnetic resonance in solution.
Author(s) -
Erik R. P. Zuiderweg,
Robert Kaptein,
Kurt Wüthrich
Publication year - 1983
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.80.19.5837
Subject(s) - lac repressor , repressor , dna , dna binding domain , sequence (biology) , protein secondary structure , nuclear magnetic resonance , helix turn helix , peptide sequence , hmg box , protein structure , nuclear magnetic resonance spectroscopy , binding site , crystallography , chemistry , binding domain , biophysics , dna binding protein , biology , physics , biochemistry , lac operon , gene , transcription factor , plasmid
A recently proposed approach for spatial structure determination in noncrystalline proteins by nuclear magnetic resonance was applied to the lac repressor DNA-binding domain. On the basis of sequence-specific 1H NMR assignments, the location of alpha-helices in the amino acid sequence was determined from nuclear Overhauser enhancement data and from amide proton exchange studies. These investigations provide detailed experimental data on the structure of a noncrystalline DNA-binding protein. The results support the hypothesis advanced by others that sequence-specific interactions between lac repressor and DNA are mediated by a particular spatial arrangement of two alpha-helices common to various different DNA-binding proteins.