Sequence Analysis and Functional Interpretation of α-Amylase Receptor from Anopheles albimanus Using a Molecular Model

Shi Ping Shan; Dong Xia Du; De Yuan Zhang; Zhao Hui Guo

doi:10.4028/www.scientific.net/AMR.798-799.1095

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Sequence Analysis and Functional Interpretation of α-Amylase Receptor from Anopheles albimanus Using a Molecular Model
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HomeAdvanced Materials ResearchAdvanced Materials Research Vols. 798-799Sequence Analysis and Functional Interpretation of...

Sequence Analysis and Functional Interpretation of α-Amylase Receptor from Anopheles albimanus Using a Molecular Model

Abstract:

Activated toxins interact with α-amylase receptor on the brush border membrane vesicle (BBMV) of the midgut epithelium, which activates intracellular oncotic pathways and leads to cell death. In order to decipher the mechanism of process how toxins interact with their receptors, it is essential to investigate their three-dimensional structure. The three-dimensional structure of α-amylase was constructed by homology modeling, based on crystal structure of Bacillus cereus oligo-1,6-glucosidase and the model was further evaluated using PROSA energy and ERRAT. The substrate binding pocket responsible for the interactions with toxins was predicted and analyzed, and the important role of binding of toxin to binding pocket on α-amylase was discussed in the aspect of Cry4Ba and Cry11Aa toxicity.

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Periodical:

Advanced Materials Research (Volumes 798-799)

Pages:

1095-1098

DOI:

https://doi.org/10.4028/www.scientific.net/AMR.798-799.1095

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Online since:

September 2013

Authors:

Shi Ping Shan, Dong Xia Du, De Yuan Zhang, Zhao Hui Guo

Keywords:

Anopheles albimanus, Binding Pocket, Homology Modeling, Midgut Epithelium, α-Amylase

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