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Crystal structure of the P2X4 receptor from zebrafish in the presence of CTP at 2.8 AngstromsCrystal structure of the P2X4 receptor from zebrafish in the presence of CTP at 2.8 Angstroms
Structural highlights
Publication Abstract from PubMedP2X receptors are trimeric ATP-gated cation channels involved in diverse physiological processes, ranging from muscle contraction to nociception. Despite the recent structure determination of the ATP-bound P2X receptors, the molecular mechanism of the nucleotide base specificity has remained elusive. Here, we present the crystal structure of zebrafish P2X4 in complex with a weak affinity agonist, CTP, together with structure-based electrophysiological and spectroscopic analyses. The CTP-bound structure revealed a hydrogen bond, between the cytosine base and the side chain of the basic residue in the agonist binding site, which mediates the weak but significant affinity for CTP. The cytosine base is further recognized by two main chain atoms, as in the ATP-bound structure, but their bond lengths seem to be extended in the CTP-bound structure, also possibly contributing to the weaker affinity for CTP over ATP. This work provides the structural insights for the nucleotide base specificity of P2X receptors. Structural insights into the nucleotide base specificity of P2X receptors.,Kasuya G, Fujiwara Y, Tsukamoto H, Morinaga S, Ryu S, Touhara K, Ishitani R, Furutani Y, Hattori M, Nureki O Sci Rep. 2017 Mar 23;7:45208. doi: 10.1038/srep45208. PMID:28332633[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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