Structural highlights
Function
[AT2A1_RABIT] This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction (By similarity).
Publication Abstract from PubMed
Biselyngbyasides (BLSs), macrolides from a marine cyanobacterium, are cytotoxic natural products whose target molecule is unknown. Here we report that BLSs are high affinity (Ki approximately 10 nM) inhibitors of Ca(2+)-pumps with a unique binding mode. The crystal structures of the Ca(2+)-pump in complex with BLSs at 3.2-3.5 A-resolution 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.
Biselyngbyasides, cytotoxic marine macrolides, are novel and potent inhibitors of the Ca(2+) pumps with a unique mode of binding.,Morita M, Ogawa H, Ohno O, Yamori T, Suenaga K, Toyoshima C FEBS Lett. 2015 Jun 4;589(13):1406-11. doi: 10.1016/j.febslet.2015.04.056. Epub, 2015 May 6. PMID:25957767[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Morita M, Ogawa H, Ohno O, Yamori T, Suenaga K, Toyoshima C. Biselyngbyasides, cytotoxic marine macrolides, are novel and potent inhibitors of the Ca(2+) pumps with a unique mode of binding. FEBS Lett. 2015 Jun 4;589(13):1406-11. doi: 10.1016/j.febslet.2015.04.056. Epub, 2015 May 6. PMID:25957767 doi:http://dx.doi.org/10.1016/j.febslet.2015.04.056
