A substrate-driven allosteric switch that enhances PDI catalytic activity
A substrate-driven allosteric switch that enhances PDI catalytic activity
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Author / Creator
Lawrence Berkeley National Lab (LBNL), Berkeley, CA (United States) , Bekendam, Roelof H. , Bendapudi, Pavan K. , Lin, Lin , Nag, Partha P. , Pu, Jun , Kennedy, Daniel R. , Feldenzer, Alexandra , Chiu, Joyce , Cook, Kristina M. , Furie, Bruce , Huang, Mingdong , Hogg, Philip J. and Flaumenhaft, Robert
Publisher
London: Nature Publishing Group UK
Journal title
Language
English
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Publication information
Publisher
London: Nature Publishing Group UK
Subjects
More information
Scope and Contents
Contents
Protein disulfide isomerase (PDI) is an oxidoreductase essential for folding proteins in the endoplasmic reticulum. The domain structure of PDI is
a
–
b
–
b′
–
x
–
a′
, wherein the thioredoxin-like
a
and
a′
domains mediate disulfide bond shuffling and
b
and
b′
domains are substrate binding. The<...
Alternative Titles
Full title
A substrate-driven allosteric switch that enhances PDI catalytic activity
Authors, Artists and Contributors
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Primary Identifiers
Record Identifier
TN_cdi_doaj_primary_oai_doaj_org_article_98add86409e74be283e23770f1a6f0cb
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_98add86409e74be283e23770f1a6f0cb
Other Identifiers
ISSN
2041-1723
E-ISSN
2041-1723
DOI
10.1038/ncomms12579
