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Divalent cations influence the dimerization mode of murine S100A9 protein by modulating its disulfide bond pattern

J Struct Biol. 2020-12; 
Luca Signor, Theo Paris, Caroline Mas, Adrien Picard, Georges Lutfalla, Elisabetta Boeri Erba, Laure Yatime
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GenParts™ DNA Fragments … coli, was synthesized by Genscript and further cloned into the NcoI – HindIII fragment of vector pETM11 (EMBL vector collection). The protein sequence of the mS100A9 sample obtained with this construct after purification is indicated in Supplementary Table S1. A theoretical … Get A Quote

摘要

S100A9, with its congener S100A8, belongs to the S100 family of calcium-binding proteins found exclusively in vertebrates. These two proteins are major constituents of neutrophils. In response to a pathological condition, they can be released extracellularly and become alarmins that induce both pro- and anti-inflammatory signals, through specific cell surface receptors. They also act as antimicrobial agents, mainly as a S100A8/A9 heterocomplex, through metal sequestration. The mechanisms whereby divalent cations modulate the extracellular functions of S100A8 and S100A9 are still unclear. Importantly, it has been proposed that these ions may affect both the ternary and quaternary structure of these proteins, the... More

关键词

Disulfide bridges, Divalent cations, Mass spectrometry, S100 proteins, X-ray crystallography