1hom
From Proteopedia
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DETERMINATION OF THE THREE-DIMENSIONAL STRUCTURE OF THE ANTENNAPEDIA HOMEODOMAIN FROM DROSOPHILA IN SOLUTION BY 1H NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY
Overview
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.
About this Structure
1HOM is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.
Reference
Determination of the three-dimensional structure of the Antennapedia homeodomain from Drosophila in solution by 1H nuclear magnetic resonance spectroscopy., Billeter M, Qian Y, Otting G, Muller M, Gehring WJ, Wuthrich K, J Mol Biol. 1990 Jul 5;214(1):183-97. PMID:2164583
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