一种新型his4型锌指肽的工程、结构和DNA结合特性。

Nucleic acids symposium series Pub Date : 2000-01-01 DOI:10.1093/nass/44.1.295

Y Hori, K Suzuki, Y Okuno, M Nagaoka, S Futaki, Y Sugiura

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引用次数: 1

摘要

我们利用转录因子Sp1中cys2his2型锌指的Cys- >His突变，构建了一种新的H4Sp1型锌指蛋白。CD和NMR研究表明，His4结构域具有Zn(II)依赖的折叠性质，二级结构与野生型Cys2His2结构域相似。DNA结合实验表明，H4Sp1能够以特定的方式结合DNA。目前的人造肽H4Sp1将为金属肽与DNA相互作用提供有价值的信息。

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The engineering, structure, and DNA binding properties of a novel His4-type zinc finger peptide.

We have created a novel His4-type zinc finger protein (H4Sp1) engineered by Cys-->His mutations of the Cys2His2-type zinc finger in transcription factor Sp1. The CD and NMR studies reveal that the His4 domain has Zn(II)-dependent folding properties and similar secondary structures to wild-type Cys2His2 domain. The DNA binding experiments demonstrate that H4Sp1 can bind DNA in a specific way. The present artificial peptide H4Sp1 will provide valuable information about the interaction between a metallopeptide and DNA.

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Nucleic acids symposium series

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