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This study describes a new artificial<jats:italic>\u03b2<\/jats:italic>-trefoil lectin that recognises Burkitt\u2019s lymphoma cells, and which was designed with the intention of finding a basis for novel cancer treatments or diagnostics. The new protein, called \u201cMitsuba\u201d, is based on the structure of the natural shellfish lectin MytiLec-1, a member of a small lectin family that uses unique sequence motifs to bind<jats:italic>\u03b1<\/jats:italic>-D-galactose. The three subdomains of MytiLec-1 each carry one galactose binding site, and the 149-residue protein forms a tight dimer in solution. Mitsuba (meaning \u201cthree-leaf\u201d in Japanese) was created by symmetry constraining the structure of a MytiLec-1 subunit, resulting in a 150-residue sequence that contains three identical tandem repeats. Mitsuba-1 was expressed and crystallised to confirm the X-ray structure matches the predicted model. Mitsuba-1 recognises cancer cells that express globotriose (Gal<jats:italic>\u03b1<\/jats:italic>(1,4)Gal<jats:italic>\u03b2<\/jats:italic>(1,4)Glc) on the surface, but the cytotoxicity is abolished.<\/jats:p>","DOI":"10.1038\/s41598-017-06332-7","type":"journal-article","created":{"date-parts":[[2017,7,13]],"date-time":"2017-07-13T15:57:43Z","timestamp":1499961463000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":43,"title":["Computational design of a symmetrical \u03b2-trefoil lectin with cancer cell binding activity"],"prefix":"10.1038","volume":"7","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-1467-2188","authenticated-orcid":false,"given":"Daiki","family":"Terada","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arnout R. 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