学术
摘 要:
利用同源建模得到杀虫晶体蛋白Cry1Ac的三维结构，之后模拟其与配体N-已酰半乳糖胺的对接，预测关键的氨基酸残基：N482、Q506、S501、L505和V483。Cry1Ac的虚拟突变体与N-已酰半乳糖胺之间的分子对接分析结果表明，R466、R468、R470和R472可能对维持Cry1Ac的DomainⅢ稳定构象起着重要作用。N482和Q506两个残基均含有酰氨基，在对接中易于形成多个氢键，这对稳定对接具有重要作用。研究结果可提供一些有用的信息，用于指导杀虫晶体蛋白的理性设计。[著者文摘]
文章出处:
《江西农业大学学报》-2008年30卷1期 -112-118页
栏目信息:
分 类 号:
文献标识码:
A
文章编号:
1000-2286（2008）01-0112-07
A Study on the Molecular Docking of Insecticidal Crystal Protein CrylAc and Its Receptor N- acetylgalactosamine
LIN Yi, ZHANG Tong - wu, CHEN Zhi -shan （Department of Bioengineering ＆ Biotechnology, Huaqiao University, Quanzhou 362021 ,China）
Abstract:
The 3 -D structure of insecticidal crystal protein Cry1Ac was constructed by homology modeling. The potential docking active cavity was predicted. Molecular docking was simulated between CrylAc and its receptor N -galactosamine. The key residues, N482, Q506, S501, L505 and V483, were predicted. Resuits from the docking simulation between virtual Cry1Ac mutant and N -galactosamine indicated that residues R466, R468, R470 and R472 were important for maintaining a stable conformation of the Domain Ⅲ. N482 and Q506 are liable to form multiple hydrogen bonds, thus are important for a stable docking. The available results in this paper gave helpful imformation for the rational design of insecticidal crystal protein.[著者文摘]
Key words:
insecticidal crystal protein ; molecular docking; homology modeling ; key amino acid
基金资助:
国家自然科学基金项目（40601046）、福建省高等学校新世纪优秀人才支持计划资助项目和福建省自然科学基金项目（B0510011）
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