Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/11448
Title: Homology modeling deduced 3D structure of the Cry1Ab22 toxin
Authors: Kashyap, S
Singh, B D
Amla, D V
Keywords: 3D structure
Homology modelling
Cry1Ab22
Bacillus thuringiensis
Issue Date: Apr-2011
Publisher: NISCAIR-CSIR, India
Abstract: -Endotoxin Cry1Ab22 is produced by Bacillus thuringiensis BtS2491Ab. The toxic spectrum of this protein is reported to span Lepidopteron and Dipteran. Here, we predict the theoretical structural model of newly reported Cry1Ab22 toxin by homology modeling method on the structure of the Cry1Aa toxin. Proposed model resembles the target by sharing common three dimensional, three domain structure. The main differences being located in the length of loops, absence of helixes (7b, 10a, 10b,11a) and presence of additional components 21, 9b). Few of the components like 9a,9b and 12a are positioned spatially at different locations. A better understanding of the 3D structure will be helpful in designing the domain swapping and mutagenesis experiments aimed at improving toxicity, and will lead to a deeper understanding of the common mechanism of toxins.
Description: 202-206
URI: http://hdl.handle.net/123456789/11448
ISSN: 0975-0967 (Online); 0972-5849 (Print)
Appears in Collections:IJBT Vol.10(2) [April 2011]

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