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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