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Blocking the interaction between S100A9 protein and RAGE V domain using S100A12 protein
1Department of Chemistry, National Tsing Hua University, Hsinchu, Taiwan.
Plos One
|June 15, 2018
Summary
The S100A12 protein inhibits S100A9 from binding to the RAGE V-domain. This discovery suggests S100A12 could be an antagonist for S100A9, potentially aiding in anti-cancer drug development.
Area of Science:
- Biochemistry
- Molecular Biology
- Structural Biology
Background:
- S100A9 and S100A12 are calcium-binding proteins involved in cellular processes.
- The V domain of Receptor for Advanced Glycation End products (RAGE) is critical for S100A9 binding, influencing cell proliferation.
Purpose of the Study:
- To investigate the interaction between S100A9 and S100A12.
- To determine if S100A12 affects the binding of S100A9 to the RAGE V-domain.
Main Methods:
- Fluorescence spectroscopy and Nuclear Magnetic Resonance (NMR) spectroscopy were employed to analyze S100A9-S100A12 interactions.
- Binary complex models were generated using 1H-15N HSQC NMR titrations and the HADDOCK program.
Main Results:
- S100A12 was shown to hinder the binding of S100A9 to the RAGE V-domain.
- Structural modeling confirmed that S100A12 physically blocks the S100A9-RAGE V-domain interaction site.
Conclusions:
- S100A12 acts as an antagonist to S100A9 by preventing its interaction with RAGE.
- These findings offer potential for developing novel anti-cancer therapeutics targeting the S100 protein family.
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