Inter- and intrasubunit interactions between transmembrane helices in the open state of P2X receptor channels.

ABSTRACT: P2X receptor channels open in response to the binding of extracellular ATP, a property that is essential for purinergic sensory signaling. Apo and ATP-bound X-ray structures of the detergent-solubilized zebrafish P2X4 receptor provide a blueprint for receptor mechanisms but unexpectedly showed large crevices between subunits within the transmembrane (TM) domain of the ATP-bound structure. Here we investigate both intersubunit and intrasubunit interactions between TM helices of P2X receptors in membranes using both computational and functional approaches. Our results suggest that intersubunit crevices found in the TM domain of the ATP-bound crystal structure are not present in membrane-embedded receptors but substantiate helix interactions within individual subunits and identify a hot spot

SUBMITTER: Heymann G 

PROVIDER: S-EPMC3801033 | biostudies-literature | 2013 Oct

REPOSITORIES: biostudies-literature