Freedman, R.B. and Klappa, P. and Ruddock, L.W. (2002) Protein disulfide isomerases exploit synergy between catalytic and specific binding domains. EMBO reports, 3 (2). pp. 136-140. ISSN 1469-221X.
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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.
|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:||08 Jun 2012 13:19|
|Resource URI:||http://kar.kent.ac.uk/id/eprint/3957 (The current URI for this page, for reference purposes)|
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