A link between ASBT and cholesterol in the blood has surfaced, but the exact mechanisms have not yet been explored. Due to the nature of protein function being inexplicably linked with their structures, X-ray crystallographic analysis of the protein may yield information on the process in which inhibition of ASBT results in lowered cholesterol levels in the blood.
ASBT is a prospective target for drugs treating
hypercholesterolemia. It may be possible to exploit the protein to transport various molecules and compounds coupled to a bile
acid, including anti-viral and cytostatic drugs.
The aims of this paper were to:
- Elucidate the structure of the protein; identify transmembrane helices and loop domains to learn how the substrate binds
- Locate catalytically important residues
- Learn how binding of the substrate causes conformational changes
- Find out how these properties can be exploited to design drugs that treat disease
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