Crystal structure of Arabidopsis thaliana calmodulin7 and insight into its mode of DNA binding.
[No authors listed]
摘要
Calmodulin (CaM) is a Ca(2+) sensor that participates in several cellular signalling cascades by interacting with various targets, including DNA. It has been shown that Arabidopsis thaliana CaM7 (AtCaM7) interacts with Z-box DNA and functions as a transcription factor [1, 2]. The crystal structure of AtCaM7, and a model of the AtCAM7-Z-box complex suggest that Arg-127 determines the DNA-binding ability by forming crucial interactions with the guanine base. We validated the model using biolayer interferometry, which confirmed that AtCaM7 interacts with Z-box DNA with high affinity. By contrast, the AtCaM2/3/5 isoform does not show any binding, although it differs from AtCaM7 by only a single residue. This article is protected by copyright. All rights reserved.
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基因功能
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原始数据
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文献解读
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