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The pro region of BPTI facilitates folding.

Abstract：

:The in vitro folding pathway of bovine pancreatic trypsin inhibitor (BPTI) has been described previously in terms of the disulfide-bonded intermediates that accumulate during folding of the protein. Folding is slow, occurring in hours at pH 7.3, 25 degrees C. In addition, approximately half of the BPTI molecules become trapped as a dead-end, native-like intermediate. In vivo, BPTI is synthesized as a precursor protein that includes a 13 residue amino-terminal pro region. This pro region contains a cysteine residue. We find that, in vitro, both the rate of formation and the yield of properly folded BPTI are increased substantially in a recombinant model of pro-BPTI. The cysteine residue is necessary for this effect. Moreover, a single cysteine residue, tethered to the carboxy-terminal end of BPTI with a flexible linker of repeating Ser-Gly-Gly residues, is sufficient to assist in disulfide formation. Thus, the pro region appears to facilitate folding by providing a tethered, solvent-accessible, intramolecular thiol-disulfide reagent.

journal_name

Cell

journal_title

Cell

authors

Weissman JS,Kim PS

doi

10.1016/0092-8674(92)90559-u

subject

Has Abstract

pub_date

1992-11-27 00:00:00

pages

841-51

issue

5

eissn

0092-8674

issn

1097-4172

pii

0092-8674(92)90559-U

journal_volume

71

pub_type

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