Biology:P2RX2
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Short description: Protein-coding gene in the species Homo sapiens
Generic protein structure example |
P2X purinoceptor 2 is a protein that in humans is encoded by the P2RX2 gene.[1][2][3]
The product of this gene belongs to the family of purinoceptors for ATP. This receptor functions as a cation conducting ligand-gated ion channel. Binding to ATP mediates synaptic transmission between neurons and from neurons to smooth muscle. Six transcript variants encoding six distinct isoforms have been identified for this gene.[3]
References
- ↑ "Molecular and functional characterization of human P2X(2) receptors". Mol Pharmacol 56 (6): 1171–81. Dec 1999. doi:10.1124/mol.56.6.1171. PMID 10570044.
- ↑ "New structural motif for ligand-gated ion channels defined by an ionotropic ATP receptor". Nature 371 (6497): 519–23. Oct 1994. doi:10.1038/371519a0. PMID 7523952. Bibcode: 1994Natur.371..519B.
- ↑ 3.0 3.1 "Entrez Gene: P2RX2 purinergic receptor P2X, ligand-gated ion channel, 2". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=22953.
Further reading
- North RA (2002). "Molecular physiology of P2X receptors". Physiol. Rev. 82 (4): 1013–67. doi:10.1152/physrev.00015.2002. PMID 12270951.
- "Atomic force microscopy imaging demonstrates that P2X2 receptors are trimers but that P2X6 receptor subunits do not oligomerize". J. Biol. Chem. 280 (11): 10759–65. 2005. doi:10.1074/jbc.M412265200. PMID 15657042.
- "Selective modulation of ligand-gated P2X purinoceptor channels by acute hypoxia is mediated by reactive oxygen species". Mol. Pharmacol. 66 (6): 1525–35. 2005. doi:10.1124/mol.104.000851. PMID 15331767.
- "Trimeric architecture of homomeric P2X2 and heteromeric P2X1+2 receptor subtypes". J. Mol. Biol. 342 (1): 333–43. 2004. doi:10.1016/j.jmb.2004.06.092. PMID 15313628.
- "Cross-talk and co-trafficking between rho1/GABA receptors and ATP-gated channels". J. Biol. Chem. 279 (8): 6967–75. 2004. doi:10.1074/jbc.M307772200. PMID 14660627.
- "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. 2003. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
- "ATP-gated ion channels assembled from P2X2 receptor subunits in the mouse cochlea". NeuroReport 13 (15): 1979–84. 2003. doi:10.1097/00001756-200210280-00030. PMID 12395104.
- "State-dependent cross-inhibition between transmitter-gated cation channels". Nature 406 (6794): 405–10. 2000. doi:10.1038/35019066. PMID 10935636. Bibcode: 2000Natur.406..405K. https://authors.library.caltech.edu/56190/3/fig2.pdf.
- "Desensitization of the P2X(2) receptor controlled by alternative splicing". FEBS Lett. 404 (2–3): 294–8. 1997. doi:10.1016/S0014-5793(97)00128-2. PMID 9119082.
- "Coexpression of P2X2 and P2X3 receptor subunits can account for ATP-gated currents in sensory neurons". Nature 377 (6548): 432–5. 1995. doi:10.1038/377432a0. PMID 7566120. Bibcode: 1995Natur.377..432L.
External links
- P2RX2+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
Original source: https://en.wikipedia.org/wiki/P2RX2.
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