P53蛋白质N末端的二级结构预测及其三维构象  

SECONDARY STRUCTURE PREDICTION OF P53 PROTEIN N-TERMINAL AND ITS 3-DIMENSIONAL CONFORMATION

作　　者：张彦[1,2] 刘次全 

机构地区：[1]昆明医学院 [2]云南大学现代生物学中心 [3]中国科学院昆明动物研究所

出　　处：《生物物理学报》1998年第4期743-749,共7页Acta Biophysica Sinica

摘　　要：以编码Ｐ５３Ｎ末端１２０个残基的ｍＲＮＡ二级结构为基础，结合Ｃｈｏｕ－Ｆａｓｍａｎ蛋白质二级结构预测原则，预测出Ｐ５３蛋白质Ｎ端的９３个残基包含四段α螺旋结构（１４－２６；３８－４６；５１－５６；６８－７０），没有发现β片层。与四种以多重序列联配为基础的蛋白质二级结构预测方法（准确率均为７３．２０％左右）相对照，结果十分相近。在ＳＧＩ工作站上以此为初始结构建立的三维构象提示，Ｐ５３Ｎ末端前８０个氨基酸肽段呈弧型板块结构，其转录激活区由两段主要螺旋组成，呈上下构形，占据弧型板块的顶部及底部外侧缘。Ｃ端１３个富含脯氨酸肽段则呈弯曲松散状。The secondary structure of the P53 protein N-terminal 93 residues was predicted based on its mRNA secondary structure template and Chou-Fasman's protein secondary structure principle of prediction. It was forecasted that there were fourαhelix (14-26, 38-46, 51-56, 68-70) in the P53 N-terminal region, and noβsheet was found. The result conformed with those obtained with the other four methods for protein secondary structure prediction that were based on the multiple alignment (accuracy～73.20%). Its three dimensional conformation was built by the SGI Indigo2 computer. It was found that the whole P53 N-terminal formed an arc plank structure and its transactive domain included two mainαhelices which constructed a top and base conformation. The rich proline peptide appeared as a loose, curve conformation. These structures corresponded well with the biological functions of P53 N-terminal.

关 键 词：P53蛋白质 MRNA二级结构 二级结构 三维构象 

分 类 号：Q510.1[生物学—生物化学]