Protein disulfide isomerases exploit synergy between catalytic and specific binding domains.

ABSTRACT: Protein disulfide isomerases (PDIs) catalyse the formation of native disulfide bonds in protein folding pathways. The key steps involve disulfide formation and isomerization in compact folding intermediates. The high-resolution structures of the a and b domains of PDI are now known, and the overall domain architecture of PDI and its homologues can be inferred. The isolated a and a' domains of PDI are good catalysts of simple thiol-disulfide interchange reactions but require additional domains to be effective as catalysts of the rate-limiting disulfide isomerizations in protein folding pathways. The b' domain of PDI has a specific binding site for peptides and its binding properties differ in specificity between members of the PDI family. A model of PDI function can be deduced in which the

SUBMITTER: Freedman RB 

PROVIDER: S-EPMC1083976 | biostudies-literature | 2002 Feb

REPOSITORIES: biostudies-literature