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

Freedman, Robert and Klappa, Peter and Ruddock, Lloyd W (2002) Protein disulfide isomerases exploit synergy between catalytic and specific binding domains. EMBO Reports, 3 (2). pp. 136-140. ISSN 1469-221X. (The full text of this publication is not available from this repository)

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Official URL
http://dx.doi.org/10.1093/embo-reports/kvf035

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.

Item Type: Review
Subjects: Q Science > Q Science (General)
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences > Protein Science Group
Depositing User: Peter Klappa
Date Deposited: 01 Sep 2008 16:05
Last Modified: 23 Apr 2014 11:42
Resource URI: http://kar.kent.ac.uk/id/eprint/3957 (The current URI for this page, for reference purposes)
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