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Title

Differences in structural elements of Bcr-Abl oncoprotein isoforms in Chronic Myelogenous Leukemia 

 

Authors

Abdul Hai1, Nadeem A Kizilbash1*, Syeda Huma H Zaidi2, Jamal Alruwaili1 & Khuram Shahzad3*

 

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

 

Email

fsd707@gmail.com; *Corresponding author

 

Article Type

Hypothesis

 

Date

Received January 01, 2014; Revised January 11, 2014; Accepted January 12, 2014; Published March 19, 2014

 

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.

 

Citation

Hai  et al Bioinformation 10(3): 108-114 (2014)
 

Edited by

P Kangueane

 

ISSN

0973-2063

 

Publisher

Biomedical Informatics

 

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.