Structural Motif and Characteristics of the Extracellular Domain of P_2XReceptors

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• 作者：Hansen ; Mitchell A. ; Barden ; Julian A. ; Balcar ; Vladimir J. ; Keay ; Kevin A. ; Bennett ; Maxwell R.
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：1997
• 出版时间：July 30, 1997
• 年：1997
• 卷：236
• 期：3
• 页码：670-675
• 全文大小：457 K

文摘

Seven sequences of the proteins recently cloned from rat tissues and identified as P_2Xreceptors are examined. Their putative transmembrane and extracellular domains and the most probable locations of disulphide bridges are discussed. Some surface accessible regions are identified and the structure of the putative ATP binding domain is discussed in the light of known selectivities and physiological characteristics of individual P_2Xsubunits. The summarised information and the theoretical considerations regarding the protein structure of P_2Xreceptors have been used to select amino acid sequences for raising antibodies against the P_2X1receptor subunit. Initial results suggest that, in rat brainstem, P_2X1receptor subunits are found on a distinct subpopulation of neuronal perikarya in distributions consistent with distributions of known α,β-methylene-ATP autoradiography and physiological effects of purinoceptor activation.