Blomqvist A G, Roubos E W, Larhammar D, Martens G J
Department of Medical Genetics, Uppsala University, Sweden.
Biochim Biophys Acta. 1995 Apr 26;1261(3):439-41. doi: 10.1016/0167-4781(95)00051-h.
Neuropeptide Y (NPY) and peptide YY (PYY) are structurally related peptides that share at least two distinct receptors denoted Y1 and Y2. The Y1 receptor has previously been cloned in man, rat and mouse. We describe here the cloning and sequence of a Xenopus laevis Y1 receptor that shares 81% amino acid sequence identity with the human receptor in the region spanning transmembrane (TM) regions I to VII. The extracellular amino-terminal part, TM IV and the second extracellular loop contain several replacements suggesting that these portions have no or limited direct interactions with the peptide ligands. The intracellular regions including the carboxy-terminal tail are nearly identical between Xenopus and mammals, suggesting strong structural constraints on the portions that may interact with G proteins.
神经肽Y(NPY)和肽YY(PYY)是结构相关的肽,它们共享至少两种不同的受体,分别称为Y1和Y2。Y1受体先前已在人、大鼠和小鼠中克隆出来。我们在此描述非洲爪蟾Y1受体的克隆及序列,在跨膜(TM)区域I至VII的区域中,该受体与人类受体的氨基酸序列同一性为81%。细胞外氨基末端部分、TM IV和第二个细胞外环包含多个置换,这表明这些部分与肽配体没有或仅有有限的直接相互作用。包括羧基末端尾巴在内的细胞内区域在非洲爪蟾和哺乳动物之间几乎相同,这表明对可能与G蛋白相互作用的部分存在强烈的结构限制。