A happy ending?

In summary, in April 2012 Hattori and Gouaux published a scientific paper. In the paper they presented new crystal structures of the P2X4 receptor in the presence and absence of ATP at atomic resolution.

They discovered that in the presence of ATP the channel had an open pore conformation and revealed an unusual ATP binding site. They characterised this novel ATP binding site. 

Next, through comparison with the structure of the P2X4 receptor not bound to ATP they were able to propose the conformational steps involved in channel activation.

This may bring our explanation of Hattori and Gouaux's 2012 paper to a close, but the story of the P2X4 receptor is far from over. 

Thanks to Kawate, Hattori and Gouaux the doors have been opened to a new 'post structural era' of research. Our new found knowledge can be used to design novel and more effective drugs that specifically target the ATP binding site or specific stages in the activation mechanism of P2X receptors to treat inflammation and chronic pain. 

There is no doubt that Hattori and Gouaux's work marks a breakthrough for the P2X receptor research community and will pave the way for new therapeutics. However, there is much still to be understood about this mysterious family of receptors. Until the next installment comes along, we leave you with a few teasers, adapted from the review of a cleverer man than you and I, on what to expect from the P2X community in the future...


What effect do the N and C termini have on the structure of the P2X4 receptor?


Why does sensitivity to agonist and antagonist differ between receptors?


Why do some receptors desensitise to ATP before others?


What are the differences between the P2X4 zebrafish receptor and receptors in other organisms?

For now, THE END.