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The structure of the antennapedia homeodomain determined by NMR-spectroscopy in solution - comparison with prokaryotic repressors

Academic Article
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Overview

authors

  • Qian, Y. Q.
  • Billeter, M.
  • Otting, G.
  • Muller, M.
  • Gehring, W. J.
  • Wuthrich, Kurt

publication date

  • November 1989

journal

  • Cell  Journal

abstract

  • The structure of the Antennapedia homeodomain from Drosophila melanogaster was determined by nuclear magnetic resonance spectroscopy in solution. It includes three well-defined helices (residues 10-21, 28-38, and 42-52) and a more flexible fourth helix (residues 53-59). Residues 30-50 form a helix-turn-helix motif virtually identical to those observed in various prokaryotic repressors. Further comparisons of the homeodomain with prokaryotic repressors showed that there are also significant differences in the molecular architectures. Overall, these studies support the view that the third helix of the homeodomain may function as the DNA recognition site. The elongation of the third helix by the fourth helix is a structured element that so far appears to be unique to the Antennapedia homeodomain.

subject areas

  • Animals
  • Drosophila melanogaster
  • Genes, Homeobox
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Protein Conformation
  • Repressor Proteins
  • Transcription Factors
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Identity

International Standard Serial Number (ISSN)

  • 0092-8674

Digital Object Identifier (DOI)

  • 10.1016/0092-8674(89)90040-8

PubMed ID

  • 2572329
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Additional Document Info

start page

  • 573

end page

  • 580

volume

  • 59

issue

  • 3

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