Solution NMR structure of zinc finger 4 and 5 from human INSM1, an essential regulator of neuroendocrine differentiation |
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| Authors: | Jiang Zhu Huapu Wang Theresa A Ramelot Michael A Kennedy Rui Hu Xiali Yue Maili Liu Yunhuang Yang |
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| Institution: | 1. State Key Laboratory of Magnetic Resonance and Atomic Molecular Physics, Wuhan Center for Magnetic Resonance, Wuhan Institute of Physics and Mathematics, Chinese Academy of Sciences, Wuhan, China;2. Department of Chemistry, College of Science, Huazhong Agricultural University, Wuhan, China;3. Department of Chemistry and Biochemistry, and the Northeast Structural Genomics Consortium, Miami University, Oxford, Ohio |
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| Abstract: | Human INSM1 containing five C‐terminal C2H2‐type zinc fingers (ZFs), is a key regulator of neuroendocrine development. Previous research reported that full‐length INSM1 containing all five ZFs recognized a consensus DNA sequence. Structure elucidation of human INSM1 ZFs is currently insufficient to understand the DNA binding mechanism. Herein, we present the solution NMR structure of ZF4‐5, in which the two ZFs adopt a head‐to‐tail arrangement and each ZF features a canonical ββα fold. NMR titrations and isothermal titration calorimetry experiments showed that ZF4‐5 binds weakly to the consensus DNA sequence. Proteins 2017; 85:957–962. © 2016 Wiley Periodicals, Inc. |
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| Keywords: | INSM1 ZF4‐5 consensus DNA solution structure mechanism |
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