Hai Abdul, Kizilbash Nadeem A, Zaidi Syeda Huma H, Alruwaili Jamal, Shahzad Khuram
Department of Biochemistry, Faculty of Medicine & Applied Medical Sciences, Northern Border University.
Department of Chemistry, Faculty of Science, Northern Border University, P.O. Box 1321, Arar-91431, Saudi Arabia.
Bioinformation. 2014 Mar 19;10(3):108-14. doi: 10.6026/97320630010108. eCollection 2014.
in silico modeling, using Psipred and ExPASy servers was employed to determine the structural elements of Bcr-Abl oncoprotein (p210(BCR-ABL)) isoforms, b2a2 and b3a2, expressed in Chronic Myelogenous Leukemia (CML). Both these proteins are tyrosine kinases having masses of 210-kDa and differing only by 25 amino acids coded by the b3 exonand an amino acidsubstitution (Glu903Asp). The secondary structure elements of the two proteins show differences in five α-helices and nine β-strands which relates to differences in the SH3, SH2, SH1 and DNA-binding domains. These differences can result in different roles played by the two isoforms in mediating signal transduction during the course of CML.
利用Psipred和ExPASy服务器进行计算机模拟，以确定慢性粒细胞白血病（CML）中表达的Bcr-Abl癌蛋白（p210(BCR-ABL)）亚型b2a2和b3a2的结构元件。这两种蛋白质都是酪氨酸激酶，质量为210 kDa，仅在由b3外显子编码的25个氨基酸和一个氨基酸取代（Glu903Asp）上有所不同。这两种蛋白质的二级结构元件在五个α螺旋和九个β链上存在差异，这与SH3、SH2、SH1和DNA结合域的差异有关。这些差异可能导致这两种亚型在CML病程中介导信号转导时发挥不同作用。
