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Protein Engineering vol. 6 no. 1 pp. 41-50, 1993
© 1993 Oxford University Press

RESEARCH-ARTICLE

Proposed structure for the DNA-binding domain of the Helix—Loop—Helix family of eukaryotic gene regulatory proteins

Toby J. Gibson, Julie D. Thompson and Ruben A. Abagyan

European Molecular Biology Laboratory Postfach 102209, Meyerhofstrasse I, W-6900 Heidelberg, Germany

A modelled tertiary structure for the dimeric HLH domain of the E47 protein is presented. Structural information was obtained from the aligned sequences of >40 members of the HLH family. The information was used to model each monomer as an {alpha}-helical hairpin, with knobs-into-holes packing of side-chains as found in antiparallel coiled-coil. The dimer forms a four-helix bundle with additional knobs-into-holes packing at the dimer interface. The size and electrostatic properties of core-forming residues are all accounted for in the model. The model does not violate any known properties of protein structure. The monomers are related by two-fold rotational symmetry, in agreement with the observed DNA-binding sites which are imperfect inverted repeats. The N-terminal basic region, in which DNA binding and base specificity reside, forms the first part of helix 1. A prediction based on the model structure is that the HLH domains do not bind to DNA in its B form but require a partially unwound conformation in order to enter the major groove.

Keywords: four-helix bundle/Helix—Loop—Helix/molecular modelling/protein structure prediction/transcriptional activator

Received May 5, 1992; revised October 7, 1992; accepted October 28, 1992.


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