1HOM
DETERMINATION OF THE THREE-DIMENSIONAL STRUCTURE OF THE ANTENNAPEDIA HOMEODOMAIN FROM DROSOPHILA IN SOLUTION BY 1H NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY
Summary for 1HOM
| Entry DOI | 10.2210/pdb1hom/pdb |
| Descriptor | ANTENNAPEDIA PROTEIN (1 entity in total) |
| Functional Keywords | dna-binding protein, dna binding protein |
| Biological source | Drosophila melanogaster (fruit fly) |
| Cellular location | Nucleus (Probable): P02833 |
| Total number of polymer chains | 1 |
| Total formula weight | 8677.16 |
| Authors | Qian, Y.-Q.,Billeter, M.,Otting, G.,Muller, M.,Gehring, W.J.,Wuthrich, K. (deposition date: 1991-10-08, release date: 1993-10-31, Last modification date: 2024-05-22) |
| Primary citation | Billeter, M.,Qian, Y.,Otting, G.,Muller, M.,Gehring, W.J.,Wuthrich, K. Determination of the three-dimensional structure of the Antennapedia homeodomain from Drosophila in solution by 1H nuclear magnetic resonance spectroscopy. J.Mol.Biol., 214:183-197, 1990 Cited by PubMed Abstract: 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. PubMed: 2164583DOI: 10.1016/0022-2836(90)90155-F PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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