Sequential 1H NMR assignment of the complex of aponeocarzinostatin with ethidium bromide and investigation of protein-drug interactions in the chromophore binding site.
Related Articles Sequential 1H NMR assignment of the complex of aponeocarzinostatin with ethidium bromide and investigation of protein-drug interactions in the chromophore binding site.
Biochemistry. 1994 Sep 6;33(35):10579-90
Authors: Mohanty S, Sieker LC, Drobny GP
Two-dimensional 1H NMR spectroscopy has been used to investigate the binding site, binding interactions, and the conformation of a 1:1 complex of aponeocarzinostatin (apo-NCS) with ethidium bromide in solution. The protein component in the complex has been sequence-specifically assigned using information derived from coherence transfer and two-dimensional homonuclear 1H NOESY experiments. The conformation of the protein in the complex has been found to be similar to the free form of the apoprotein, and intermolecular NOEs between the residues of the protein to protons on the ethidium bromide suggest that the ethidium bromide is bound to the protein in the same cleft in which the neocarzinostatin chromophore binds. Protons on ethidium show NOE interactions to the following protein residues: Trp-39, Leu-45, Cys-47, and Gln-94 which interact with the phenanthridine ring system of ethidium, Gly-102 and Asn-103 which interact with the alkyl chain of ethidium, and Phe-52 which interacts with the phenyl ring of ethidium. The orientation of ethidium in the cleft of apo-NCS is compared and contrasted to orientation of the chromophore as determined by high-resolution NMR and X-ray diffraction studies.
PMID: 8075058 [PubMed - indexed for MEDLINE]
Source:
PubMed