Protein disulfide isomerases exploit synergy between catalytic and specific binding domains |
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Authors: | Freedman Robert B Klappa Peter Ruddock Lloyd W |
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Affiliation: | Department of Biosciences, University of Kent, Canterbury CT2 7NJ, UK. r.b.freedman@ukc.ac.uk |
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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 domains function synergically: the b′ domain binds unstructured regions of polypeptide, while the a and a′ domains catalyse the chemical isomerization steps. |
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