期刊
PROTEIN JOURNAL
卷 28, 期 2, 页码 104-110出版社
SPRINGER
DOI: 10.1007/s10930-009-9169-0
关键词
Three-dimensional structure; Homology modeling; Cry5Aa; Bacillus thuringiensis
资金
- National Natural Science Foundation of China [30670052, 30570050]
- 863 Program of China [2006AA02Z187, 2006AA10A212]
Cry5Aa is a crystal protein produced by Bacillus thuringiensis serovar. damstadiensis during its stationary phase, this delta-endotoxin is active against nematodes and has (,real potential for nematodes control. The theoretical model of the three-dimensional structure of Cry5Aa was predicted by homology modeling on the structures of the Cry1Aa which is specific to Lepidopteran insects. The structure of the Cry5Aa resembles previously reported Cry toxin structures but shows the following distinctions. Cry5Aa has a long insertion in alpha 2 of domain I. Some loops in the domain II and III of Cry5Aa are exposed to the solvent. In this work we give a brief description of Our model and hypothesize the residues of the Cry5Aa that could be important in receptor recognition and pore formation. This model will be helpful for the design of mutagenesis experiments aimed to the improvement of toxicity, and lead to a deep understanding of the mechanism of action of nematicidal toxins.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据