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Title |
Differences in structural elements of Bcr-Abl oncoprotein isoforms in Chronic Myelogenous Leukemia
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Authors |
Abdul Hai1, Nadeem A Kizilbash1*, Syeda Huma H Zaidi2, Jamal Alruwaili1 & Khuram Shahzad3* |
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Affiliation |
1Department of Biochemistry, Faculty of Medicine & Applied Medical Sciences, Northern Border University; 2Department of Chemistry, Faculty of Science, Northern Border University, P.O. Box 1321, Arar-91431, Saudi Arabia; 3Illinois Informatics Institute, University of Illinois, Urbana-Champaign, Illinois, U.S.A
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fsd707@gmail.com; *Corresponding author
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Article Type |
Hypothesis
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Date |
Received January 01, 2014; Revised January 11, 2014; Accepted January 12, 2014; Published March 19, 2014
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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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Citation |
Hai et al.
Bioinformation 10(3): 108-114 (2014) |
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Edited by |
P Kangueane
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ISSN |
0973-2063
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Publisher |
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License |
This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License. |