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within the biosynthesis of peptidoglycan, a three-dimensional mesh that protects the bacterium from variations in osmotic pressure and gives it its shape. This observation led for the suggestion that bacterial a2Ms could act in partnership with PBP1c through infection, the former protecting bacteria from proteases, the latter acting in cell wall repair upon prospective disruption of the outer memb
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ther reduce non-identical domains we replaced the extracellular ligand binding domains on the receptor chimeras with that of TNFR1. This resulted in molecules identical in both their extracellular ligand binding components and their intracellular signaling domains, but unique in their TM domains and the adjacent stalk regions, i.e. the sequences connecting the TM with all the cysteine rich domains
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