The P2X1 receptor as a therapeutic target.

"fig 4 a atp-bound hp2x3 receptor with one of the atp binding locations emphasised (protein data bank: 5svk) b a close up view of the atp molecule bound to the hp2x3 receptor with the interacting residues labelled the interacting hp2x3 residues are reported in the table below with the sequence aligned p2x1 residues channel activation shares a common mechanism among p2x receptor structures in which the dorsal fin and head domains move toward each other producing a cleft closure while the left flipper domain moves away from the orthosteric binding site."

"Declarations Competing interestsThe authors declare no competing interests. Conflicts of interestThe authors declare no conflict of interest. Ethical approvalEthics approval not applicable. Informed consentAll authors agree with the content of the manuscript and with the submission. Competing interests The authors declare no competing interests. Conflicts of interest The authors declare no conflict of interest."

"Funding Open Access funding enabled and organized by CAUL and its Member Institutions"