Publication in Cell: Salipro® enables to unlock the structural dynamics of the human S1P transporter using cryoEM

Our Salipro® platform technology has enabled a breakthrough in understanding Sphingosine-1-Phosphate (S1P) biology. Researchers captured cryoEM structures of the human S1P transporter Spns2 in multiple functionally relevant states, contributing to novel insights into the transport process of S1P, a key player in immune regulation and angiogenesis.

In addition, the Salipro®-Spns2 structures revealed the binding site and the inhibitory mechanism of a specific Spns2 inhibitor (16d), accelerating the design of next-generation Spns2 modulators for treatments of cancer, inflammation, and immune diseases.

Please find more information in the original article in Cell:
H. Chen, et al., Structural and functional insights into Spns2-mediated transport of sphingosine-1-phosphate. Cell 186, 2644–2655, (2023).