{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,9]],"date-time":"2026-01-09T12:33:07Z","timestamp":1767961987424,"version":"3.49.0"},"reference-count":51,"publisher":"Wiley","issue":"18","license":[{"start":{"date-parts":[[2011,8,8]],"date-time":"2011-08-08T00:00:00Z","timestamp":1312761600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2011,9]]},"abstract":"Taenia\u2003solium<\/jats:italic> is the cestode responsible for porcine and human cysticercosis. The ability of this parasite to establish itself in the host is related to its evasion of the immune response and its antioxidant defence system. The latter includes enzymes such as cytosolic Cu\/Zn superoxide dismutase. In this article, we describe the crystal structure of a recombinant T.\u2003solium<\/jats:italic> Cu\/Zn superoxide dismutase, representing the first structure of a protein from this organism. This enzyme shows a different charge distribution at the entrance of the active channel when compared with human Cu\/Zn superoxide dismutase, giving it interesting properties that may allow the design of specific inhibitors against this cestode. The overall topology is similar to other superoxide dismutase structures; however, there are several His and Glu residues on the surface of the protein that coordinate metal ions both intra\u2010 and intermolecularly. Interestingly, one of these ions, located on the \u03b22\u2003strand, establishes a metal\u2010mediated intermolecular \u03b2\u2013\u03b2 interaction, including a symmetry\u2010related molecule. The factors responsible for the abnormal protein\u2013protein interactions that lead to oligomerization are still unknown; however, high metal levels have been implicated in these phenomena, but exactly how they are involved remains unclear. The present results suggest that this structure could be useful as a model to explain an alternative mechanism of protein aggregation commonly observed in insoluble fibrillar deposits.<\/jats:p>Database<\/jats:bold>\n \u2028The atomic coordinates and structure factors have been deposited in the Protein Data Bank under the accession number 3MND<\/jats:ext-link>.<\/jats:p>Structured digital abstract<\/jats:bold><\/jats:p>\n\u2002Cu\/Zn SOD<\/jats:ext-link>\u2003binds<\/jats:ext-link>\u2003to\u2003Cu\/Zn SOD<\/jats:ext-link> by dynamic light scattering<\/jats:ext-link>\u2003(View Interaction\u20031<\/jats:ext-link>,\u20032<\/jats:ext-link>)<\/jats:p><\/jats:list-item>\n\u2002Cu\/Zn SOD<\/jats:ext-link>\u2003binds<\/jats:ext-link>\u2003to\u2003Cu\/Zn SOD<\/jats:ext-link> by mass spectrometry studies of complexes<\/jats:ext-link>\u2003(View interaction)<\/jats:ext-link><\/jats:p><\/jats:list-item>\n\u2002Cu\/Zn SOD<\/jats:ext-link>\u2003binds<\/jats:ext-link>\u2003to\u2003Cu\/Zn SOD<\/jats:ext-link> by molecular sieving<\/jats:ext-link>\u2003(View Interaction\u20031<\/jats:ext-link>,\u20032<\/jats:ext-link>)<\/jats:p><\/jats:list-item>\n\u2002Cu\/Zn SOD<\/jats:ext-link>\u2003binds<\/jats:ext-link>\u2003to\u2003Cu\/Zn SOD<\/jats:ext-link> by x\u2010ray crystallography<\/jats:ext-link>\u2003(View interaction)<\/jats:ext-link><\/jats:p><\/jats:list-item>\n<\/jats:list><\/jats:p>","DOI":"10.1111\/j.1742-4658.2011.08247.x","type":"journal-article","created":{"date-parts":[[2011,7,18]],"date-time":"2011-07-18T12:19:32Z","timestamp":1310991572000},"page":"3308-3318","source":"Crossref","is-referenced-by-count":8,"title":["Crystal structure of Cu\u200a\/\u200aZn superoxide dismutase from Taenia\u2003solium<\/i> reveals metal\u2010mediated 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