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Here we report that BLSs are high affinity (<jats:italic>K<\/jats:italic>\n<jats:sub>i<\/jats:sub>\n\u223c 10 nM) inhibitors of Ca<jats:sup>2+<\/jats:sup>\u2010pumps with a unique binding mode. The crystal structures of the Ca<jats:sup>2+<\/jats:sup>\u2010pump in complex with BLSs at 3.2\u20133.5 \u00c5\u2010resolution show that BLSs bind to the pump near the cytoplasmic surface of the transmembrane region. The crystal structures and activity measurement of BLS analogs allow us to identify the structural features that confer high potency to BLSs as inhibitors of the pump.<\/jats:p>","DOI":"10.1016\/j.febslet.2015.04.056","type":"journal-article","created":{"date-parts":[[2015,5,6]],"date-time":"2015-05-06T16:46:07Z","timestamp":1430930767000},"page":"1406-1411","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":27,"title":["Biselyngbyasides, cytotoxic marine macrolides, are novel and potent inhibitors of the Ca<sup>2+<\/sup> pumps with a unique mode of 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