Bioinorganic Explorations of Zn(II) Sequestration by Human S100 Host-Defense Proteins
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nihms971677.pdf
Description
Accepted version
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1010.41 KB
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Adobe PDF
Checksum (MD5)
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Author(s)
Cunden, Lisa Stephanie
Nolan, Elizabeth Marie
Date Issued
January 2018
Journal
Biochemistry
Publisher
American Chemical Society (ACS)
Citation
Cunden, Lisa S., and Elizabeth M. Nolan. "Bioinorganic Explorations of Zn(II) Sequestration by Human S100 Host-Defense Proteins." Biochemistry 57, 11 (January 2018): 1673-1680 © 2018 American Chemical Society
Version
Author's final manuscript
Abstract
The human innate immune system launches a metal-withholding response to starve invading microbial pathogens of essential metal nutrients. Zn(II)-sequestering proteins of the human S100 family contribute to this process and include calprotectin (CP, S100A8/S100A9 oligomer, calgranulin A/B oligomer), S100A12 (calgranulin C), and S100A7 (psoriasin). This Perspective highlights recent advances in the Zn(II) coordination chemistry of these three proteins, as well as select studies that evaluate Zn(II) sequestration as an antimicrobial mechanism. Keywords: immunology; peptides and proteins; metals; monomersIons
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
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Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.
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DOI of Published Version
https://doi.org/10.1021/acs.biochem.7b01305
