Abstract
Trichosanthin, a type I ribosome-inactivating protein with RNAN-glycosidase activity, forms a stable complex with nicotinamide adenine dinucleotide phosphate, a substrate analog. Difference UV spectroscopy, fluorescence spectroscopy, and31P NMR are used to identify the formation of the complex, followed by a crystal structure analysis carried out to elucidate the active-site structure of trichosanthin. The determination of germinal vesicle breakdown indicates that the complex does not, at least for abortion-inducing activity, result in competitive inhibition to the protein.
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Abbreviations
- TCS:
-
trichosanthin
- RIP:
-
ribosome-inactivating protein
- NADPH:
-
nicotinamide adenine dinucleotide phosphate
- AMP:
-
adenosine 5′-mondphosphate
- ATP:
-
adenosine 5′-triphosphate
- CMP:
-
cytidine 5′-monophosphate
- GTP:
-
guanosine 5′-triphosphate
- UMP:
-
uridine 5′-monophosphate
- NADH:
-
nicotinamide adenine dinucleotide
- GVBD:
-
germinal vesicle breakdown
- HIV:
-
human immunodeficiency virus
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Xiong, JP., Xia, ZX. & Wang, Y. Identification of a stable complex of trichosanthin with nicotinamide adenine dinucleotide phosphate. J Protein Chem 14, 139–144 (1995). https://doi.org/10.1007/BF01980325
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DOI: https://doi.org/10.1007/BF01980325