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Structure determination of the antp(c39- s) homeodomain from nuclear-magnetic-resonance data in solution using a novel strategy for the structure calculation with the programs diana, caliba, habas and glomsa

Academic Article
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Overview

authors

  • Guntert, P.
  • Qian, Y. Q.
  • Otting, G.
  • Muller, M.
  • Gehring, W.
  • Wuthrich, Kurt

publication date

  • February 1991

journal

  • Journal of Molecular Biology  Journal

abstract

  • The structure of a mutant Antennapedia homeodomain, Antp(C39----S), from Drosophila melanogaster was determined using a set of new programs introduced in the accompanying paper. An input dataset of 957 distance constraints and 171 dihedral angle constraints was collected using two-dimensional n.m.r. experiments with the 15N-labeled protein. The resulting high quality structure for Antp(C39----S), with an average root-mean-square deviation of 0.53 A between the backbone atoms of residues 7 to 59 in 20 energy-refined distance geometry structures and the mean structure, is nearly identical to the previously reported structure of the wild-type Antp homeodomain. The only significant difference is in the connection between helices III and IV, which was found to be less kinked than was indicated by the structure determination for Antp. The main emphasis of the presentation in this paper is on a detailed account of the practical use of a novel strategy for the computation of nuclear magnetic resonance structures of proteins with the combined use of the programs DIANA, CALIBA, HABAS and GLOMSA.

subject areas

  • Algorithms
  • Amino Acid Sequence
  • Animals
  • Antennapedia Homeodomain Protein
  • Cysteine
  • DNA-Binding Proteins
  • Drosophila Proteins
  • Drosophila melanogaster
  • Genes, Homeobox
  • Homeodomain Proteins
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Molecular Sequence Data
  • Mutation
  • Nuclear Proteins
  • Protein Conformation
  • Serine
  • Software
  • Stereoisomerism
  • Structure-Activity Relationship
  • Thermodynamics
  • Transcription Factors
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Identity

International Standard Serial Number (ISSN)

  • 0022-2836

Digital Object Identifier (DOI)

  • 10.1016/0022-2836(91)90755-u

PubMed ID

  • 1671604
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Additional Document Info

start page

  • 531

end page

  • 540

volume

  • 217

issue

  • 3

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