John Domanick mTOR Final

John Domanick mTOR Final - John Domanick Bchm 100a 11-22-10...

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John Domanick 11-22-10 Bchm 100a Activity of Wild-Type Mammalian Target of Rapamycin Complexes Versus Truncated Catalytic Analogue The mammalian target of rapamycin (mTOR), a protein kinase which plays a major role in cell growth, is a common drug target for cancer therapies. Drug effects on biological mTOR are very difficult to characterize though, as mTOR forms two protein complexes in vivo , mTORC1 and mTORC2, which can not be easily purified in significant quantities from cells. In order to circumvent this problem, studies are conducted on a truncated version of mTOR, which retains its catalytic domain, and thus any catalytic properties. Tao et al. set out to study both the activities of biological mTOR (mTORC1 and mTORC2) and truncated mTOR, to determine the degree of enzymatic resemblance between truncated and biological versions of mTOR. This would shed light onto exactly how analogous truncated mTOR is to biological mTOR, and whether studies on truncated mTOR actually afford data medically relevant to biological mTOR. With enough resemblance between the two species, studies can be continued on truncated mTOR, with confidence that any findings will also be applicable to biological mTOR. After purifying sufficient quantities of both mTORC1 and mTORC2, Tao et al. investigated the effects of complex formation on the substrate selectivity and catalytic
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This note was uploaded on 10/06/2011 for the course BCHM 100 taught by Professor Oprian during the Fall '07 term at Brandeis.

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John Domanick mTOR Final - John Domanick Bchm 100a 11-22-10...

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