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Title
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Determination of the three-dimensional structure of the Antennapedia homeodomain from Drosophila in solution by 1H nuclear magnetic resonance spectroscopy.
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Authors
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M.Billeter,
Y.Qian,
G.Otting,
M.Müller,
W.J.Gehring,
K.Wüthrich.
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Ref.
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J Mol Biol, 1990,
214,
183-197.
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PubMed id
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Abstract
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The determination of the three-dimensional structure of the Antennapedia
homeodomain from Drosophila in solution is described. The techniques used are 1H
nuclear magnetic resonance spectroscopy for the data collection, and calculation
of the protein structure with the program DISMAN followed by restrained energy
minimization with a modified version of the program AMBER. A group of 19
conformers characterizes a well-defined structure for residues 7 to 59, with an
average root-mean-square distance from the backbone atoms of 0.6 A relative to
the mean of the 19 structures. The structure contains a helix from residues 10
to 21, a helix-turn-helix motif from residues 28 to 52, which is similar to
those reported for several prokaryotic repressor proteins, and a somewhat
flexible fourth helix from residues 53 to 59, which essentially forms an
extension of the presumed recognition helix, residues 42 to 52. The helices
enclose a structurally well-defined molecular core of hydrophobic amino acid
side-chains.
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