We determined the structure of the TASK-1 potassium ion channel. Mutations in TASK-1 are linked to pulmonary arterial hypertension.
TASK-1 has an unusual X-gate, consisting of two crossed helices. This type of gate is not present in related potassium channels and explains the low activity of TASK-1. We also crystallised TASK-1 in complex with inhibitors and found that they bind in the central cavity, trapped by the X-gate.
This work is a collaboration with Bayer AG and University of Marburg.