A substrate-driven allosteric switch that enhances PDI catalytic activity-Reference-Cited by-同舟云学术

A substrate-driven allosteric switch that enhances PDI catalytic activity

Published:2016-08-30 Issue:1 Volume:7 Page:
ISSN:2041-1723
Container-title:Nature Communications
language:en
Short-container-title:Nat Commun

Author:

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.,Flaumenhaft Robert

Publisher

Springer Science and Business Media LLC

Subject

General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry

Link

http://www.nature.com/articles/ncomms12579.pdf

Reference47 articles.

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2. Ellgaard, L. & Ruddock, L. W. The human protein disulphide isomerase family: substrate interactions and functional properties. EMBO Rep. 6, 28–32 (2005).

3. Pirneskoski, A. et al. Molecular characterization of the principal substrate binding site of the ubiquitous folding catalyst protein disulfide isomerase. J. Biol. Chem. 279, 10374–10381 (2004).

4. Freedman, R. B., Klappa, P. & Ruddock, L. W. Protein disulfide isomerases exploit synergy between catalytic and specific binding domains. EMBO Rep. 3, 136–140 (2002).

5. Darby, N. J., Penka, E. & Vincentelli, R. The multi-domain structure of protein disulfide isomerase is essential for high catalytic efficiency. J. Mol. Biol. 276, 239–247 (1998).

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