Differences in structural elements of Bcr-Abl oncoprotein isoforms in Chronic Myelogenous Leukemia |
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Authors: | Abdul Hai Nadeem A Kizilbash Syeda Huma H Zaidi Jamal Alruwaili Khuram Shahzad |
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Institution: | 1.Department of Biochemistry, Faculty of Medicine & Applied Medical Sciences, Northern Border University;2.Department of Chemistry, Faculty of Science, Northern Border University, P.O. Box 1321, Arar-91431, Saudi Arabia;3.Illinois Informatics Institute, University of Illinois, Urbana-Champaign, Illinois, U.S.A |
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Abstract: | in silico modeling, using Psipred and ExPASy servers was employed to determine the structural elements of Bcr-Abl oncoprotein
(p210BCR-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. |
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