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Volume 36 Number 3 Volume 36 Number 4 Volume 37 Number 1

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Research articles

ScienceAsia 36 (2010): 280-285 |doi: 10.2306/scienceasia1513-1874.2010.36.280

Homology modelling deduced 3-D structure of Bacillus thuringiensis Cry1Ab17 toxin

S. Kashyapa,*, B.D. Singhb, D.V. Amlac

ABSTRACT:     We predict the first theoretical structural model of the newly reported Cry1Ab17 δ-endotoxin produced by Bacillus thuringiensis using homology modelling. Both Cry1Ab17 and Cry1Aa share a common structure; both contain three flexible domains that participate in the formation of a pore and determine the receptor binding specificity. The main differences between the two is in the length of loops, and in Cry1Ab17, the absence of α7b, α10a, α10b, α12a, β19, β20 and presence of additional β0 β1b, α9b components. A few of the components such as α8a, α8b, α9a, α9b, and α11a differ in their locations. A better understanding of the 3-D structure of Cry1Ab17 will be helpful in designing the domain swapping experiments to improve its insecticidal toxicity.

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a National Bureau of Agriculturally Important Microorganisms (ICAR), Kusmaur, Kaithouli, Mau Nath Bhanjan 275101, India
b School of Biotechnology, Faculty of Science, Banaras Hindu University, Varanasi 221005 (U.P.) India
c Molecular Biology & Genetic Engineering Division, National Botanical Research Institute, Rana Pratap Marg, P.B. &hash; 436, Lucknow 226001, India

* Corresponding author, E-mail: sudhanshukshyp@gmail.com

Received 13 Mar 2010, Accepted 24 Sep 2010