| Literature DB >> 28160313 |
Jiang Zhu1, Huapu Wang1,2, Theresa A Ramelot3, Michael A Kennedy3, Rui Hu1, Xiali Yue2, Maili Liu1, Yunhuang Yang1.
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.Entities:
Keywords: INSM1; ZF4-5; consensus DNA; mechanism; solution structure
Mesh:
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Year: 2017 PMID: 28160313 PMCID: PMC5389901 DOI: 10.1002/prot.25259
Source DB: PubMed Journal: Proteins ISSN: 0887-3585