Domain wise docking analyses of the modular chitin binding protein CBP50 from <i>Bacillus thuringiensis </i>serovar konkukian S4

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Title	*Domain wise docking analyses of the modular chitin binding protein CBP50 from Bacillus thuringiensis* serovar konkukian S4**
Authors	Ujala Sehar¹, Muhammad Aamer Mehmood¹*, Khadim Hussain¹, Salman Nawaz², Shahid Nadeem³, Muhammad Hussnain Siddique¹, Habibullah Nadeem¹, Munazza Gull⁴, Niaz Ahmad⁵, Iqra Sohail¹, Saba Shahid Gill¹ & Summera Majeed¹
Affiliation	¹Department of Bioinformatics and Biotechnology, Faculty of Science & Technology, Government College University Faisalabad, Faisalabad, Pakistan; ²COMSATS Institute of Information Technology, Islamabad, Pakistan; ³Nuclear Institute for Agriculture & Biology, Faisalabad, Pakistan; ⁴Biochemistry Department, Faculty of Science, King Abdul Aziz University, Jeddah, Kingdom of Saudi Arabia; ⁵National Institute for Biotechnology & Genetic Engineering, Faisalabad-38000, Pakistan;
Email	draamer@gcuf.edu.pk; *Corresponding author
Article Type	Hypothesis
Date	Received October 04, 2013; Accepted October 19, 2013; Published November 11, 2013
Abstract	This paper presents an in silico characterization of the chitin binding protein CBP50 from B. thuringiensis serovar konkukian S4 through homology modeling and molecular docking. The CBP50 has shown a modular structure containing an N-terminal CBM33 domain, two consecutive fibronectin-III (Fn-III) like domains and a C-terminal CBM5 domain. The protein presented a unique modular structure which could not be modeled using ordinary procedures. So, domain wise modeling using MODELLER and docking analyses using Autodock Vina were performed. The best conformation for each domain was selected using standard procedure. It was revealed that four amino acid residues Glu-71, Ser-74, Glu-76 and Gln-90 from N-terminal domain are involved in protein-substrate interaction. Similarly, amino acid residues Trp-20, Asn-21, Ser-23 and Val-30 of Fn-III like domains and Glu-15, Ala-17, Ser-18 and Leu-35 of C-terminal domain were involved in substrate binding. Site-directed mutagenesis of these proposed amino acid residues in future will elucidate the key amino acids involved in chitin binding activity of CBP50 protein.
Keywords	CBP50, homology modeling, molecular docking, substrate-protein interaction.
Citation	Sehar et al. Bioinformation 9(18): 901-907 (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.