Protein folding: Prolyl isomerases join the fold
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چکیده
منابع مشابه
Protein folding: Prolyl isomerases join the fold
Cyclophilins have prolyl isomerase activity, but evidence for their suggested role in protein folding in cells has been scarce; now they have been found to accelerate the folding of mitochondrial precursor proteins.
متن کاملChaperone domains convert prolyl isomerases into generic catalysts of protein folding.
The cis/trans isomerization of peptide bonds before proline (prolyl bonds) is a rate-limiting step in many protein folding reactions, and it is used to switch between alternate functional states of folded proteins. Several prolyl isomerases of the FK506-binding protein family, such as trigger factor, SlyD, and FkpA, contain chaperone domains and are assumed to assist protein folding in vivo. Th...
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Prolyl isomerases comprise three main protein families totalling over thirty mammalian genes, and several hundred orthologues across the biological domains, with a very broad spectrum of physiological functions and disease implications. Potent small molecule inhibitors exist for members of the three main mammalian families (cyclophilins, FKBPs and parvulins),. but, until recently, these protein...
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ژورنال
عنوان ژورنال: Current Biology
سال: 1995
ISSN: 0960-9822
DOI: 10.1016/s0960-9822(95)00197-7