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作 者:崔映宇[1] 余龙[1] 龚若沫 张民[1] 范玉新[1] 傅强[1] 岳鹏 赵寿元[1]
出 处:《高技术通讯》1998年第12期1-6,共6页Chinese High Technology Letters
基 金:国家自然科学基金
摘 要:从人胎脑cDNA文库分离到一个长595bp的cDNA,它含一个编码153个氨基酸的完整开放阅读框,5UTR长18bp,3UTR长118bp;在3UTR中,含有非典型的加尾信号序列“AATTAAA”和长15bp的polyA序列。由阅读框推导的编码蛋白质的分子量为17.3KD,等电点为4.89。由于它与小鼠神经元蛋白NP15.6呈高度同源,尤其是二者的推导氨基酸序列一致性高达81.2%,故将这一新cDNA序列推导的蛋白命名为神经元蛋白P17.3。用PCGENE软件包的GGBSM程序推导该蛋白质的二级结构,发现该蛋白中32.6%的氨基酸参与组成α螺旋结构,15.0%的氨基酸参与组成β折叠片;用位点检测分析软件的PESTFIND程序分析,发现它的第48~68位氨基酸残基区为快速衰变蛋白特征性的“PEST”结构域。A full length cDNA with 595bp was isolated from a human fetal brain cDNA library. It contains an open reading frame encoding 153 amino acids, with a 18bp 5UTR and a 118bp 3UTR in which there is an atypical polyadenylation signal (AATTAAA) and a 15bp poly(A) tail. The calculated molecular weight of the deduced protein is 17.3KD. The predicted isoelectric point is 4.89. On account of its high homologue to mouse neuronal protein NP15.6 and 81.2% identity between them, the deduced protein was named neuronal protein 17.3(in short, NP17.3). When its secondary structure was examined by the GGBSM program of PCGENE software, it was found that 32.6% and 15.0% of its amino acids were involved in forming α helix and β sheet respectively. Examined by PESTFIND program, a typical PEST region of rapidly degraded protein was found in its 48~68 residues.
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