Protein folding: Prolyl isomerases join the fold

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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.

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Chaperone 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 in yeast.

Prolyl isomerases are enzymes that catalyze cis-trans isomerization of peptidyl-prolyl bonds and span three structurally unrelated protein families: the cyclophilins, FKBPs, and parvulins. The genome of the budding yeast Saccharomyces cerevisiae encodes eight different cyclophilins (Cpr1 to Cpr8), four FKBPs (Fpr1 to Fpr4), and a single parvulin (Ess1). Remarkably, two of these proteins, cyclop...

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Prolyl Isomerases and Nuclear Function

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Prolyl Isomerases as New Therapeutic Targets

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