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Proteins. 2017 Feb 03;:
Authors: Zhu J, Wang H, Ramelot TA, Kennedy MA, Hu R, Yue X, Liu M, Yang Y
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 ??? fold. NMR titrations and isothermal titration calorimetry experiments showed that ZF4-5 binds weakly to the consensus DNA sequence. This article is protected by copyright. All rights reserved.
PMID: 28160313 [PubMed - as supplied by publisher]
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NMR structure note: solution structure of human Miz-1 zinc fingers 8 to 10
NMR structure note: solution structure of human Miz-1 zinc fingers 8 to 10
NMR structure note: solution structure of human Miz-1 zinc fingers 8 to 10
Content Type Journal Article
Category NMR structure note
Pages 1-7
DOI 10.1007/s10858-012-9670-1
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