Conserved Residues Lys57 and Lys401 of Protein Disulfide Isomerase Maintain an Active Site Conformation for Optimal Activity: Implications for Post-Translational Regulation

Conserved Residues Lys57 and Lys401 of Protein Disulfide Isomerase Maintain an Active Site Conformation for Optimal Activity: Implications for Post-Translational Regulation

Despite its study since the 1960's, very little is known about the post-translational regulation of the multiple catalytic activities performed by protein disulfide isomerase (PDI), the primary protein folding catalyst of the cell. This work identifies a functional role for the highly conserved...

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Bibliographic Details
Main Authors: Cody Caba, Hyder Ali Khan, Janeen Auld, Ryo Ushioda, Kazutaka Araki, Kazuhiro Nagata, Bulent Mutus
Format: Article
Language:English
Published: Frontiers Media S.A. 2018-02-01
Series:Frontiers in Molecular Biosciences
Subjects:
lysine acetylation
oxidative protein folding
enzyme kinetics
protein disulfide isomerase
redox
thiol-disulfide exchange
Online Access:http://journal.frontiersin.org/article/10.3389/fmolb.2018.00018/full

Internet

http://journal.frontiersin.org/article/10.3389/fmolb.2018.00018/full

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