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It is involved in host\u2010parasite response, and linked to corneal autoimmune diseases connected with filarial parasite infestation. Interaction of S100A12 with a multiligand receptor for advanced glycation end products (RAGE) mediates inflammation. Human recombinant S100A12 was found to induce neuritogenesis of cultured hippocampal cells, similar to two other S100 proteins, S100B and S100A4. X\u2010ray structure of S100A12 has been solved in two crystal forms: R3 and P2<jats:sub>1<\/jats:sub>. In the R3 crystal form S100A12 is a dimer, and in the P2<jats:sub>1<\/jats:sub> crystal form the dimers are arranged as a hexamer. The hexameric form suggests its role in receptor oligomerisation. S100A12 binds copper at the predicted zinc\/copper binding site, which is located close to the surface of the protein. We propose copper\u2010mediated generation of reactive oxygen species by S100A12 as its function in host\u2010parasite response. Microsc. Res. 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