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We hypothesize that this is due to constriction of the allosteric site following transition from closed to open channel state. We propose that M109, F178, Y300, R301 and I312 are key residues for 5-BDBD binding, provide a structural explanation of how they contribute to 5-BDBD antagonism, and highlight that the limited action of 5-BDBD on open versus closed channels is due to a conformational change in the allosteric site. Significance Statement Activity of P2X4 receptor is associated with neuropathic pain, inflammation and vasodilatat