Three dimensional (3D) structure prediction and substrate-protein interaction study of the chitin binding protein CBP24 from <i>B. thuringiensis</i>

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Title	Three dimensional (3D) structure prediction and substrate-protein interaction study of the chitin binding protein CBP24 from B. thuringiensis
Authors	Ujala Sehar¹, Muhammad Aamer Mehmood¹*, Salman Nawaz², Shahid Nadeem^1,3, Khadim Hussain¹, Iqra Sohail¹, Muhammad Rizwan Tabassum¹, Saba Shahid Gill¹ & Anam Saqib¹
Affiliation	¹Department of Bioinformatics and Biotechnology, Faculty of Science & Technology, Government College University, Faisalabad, Pakistan; ²Department of Biosciences, COMSATS Institute of Information Technology, Islamabad, Pakistan; ³Nuclear Institute for Agriculture and Biology, Faisalabad, Pakistan
Email	draamer@gcuf.edu.pk; *Corresponding author
Article Type	Hypothesis
Date	Received July 24, 2013; Accepted July 25, 2013; Published August 07, 2013
Abstract	Bacillus thuringiensis is an insecticidal bacterium whose chitinolytic system has been exploited to improve insect resistance in crops. In the present study, we studied the CBP24 from B. thuringiensis using homology modeling and molecular docking. The primary and secondary structure analyses showed CBP24 is a positively charged protein and contains single domain that belongs to family CBM33. The 3D model after refinement was used to explore the chitin binding characteristics of CBP24 using AUTODOCK. The docking analyses have shown that the surface exposed hydrophilic amino acid residues Thr-103, Lys-112 and Ser-162 interact with substrate through H-bonding. While, the amino acids resides Glu-39, Tyr-46, Ser-104 and Asn-109 were shown to have polar interactions with the substrate. The binding energy values evaluation of docking depicts a stable intermolecular conformation of the docked complex. The functional characterization of the CBP24 will elucidate the substrate-interaction pathway of the protein in specific and the carbohydrate binding proteins in general leading towards the exploration and exploitation of the prokaryotic substrate utilization pathways.
Keywords	B. thuringiensis, CBP24, homology modeling, Molecular docking
Citation	Sehar et al. Bioinformation 9(14): 725-729 (2013)
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.