Solution NMR structure of zinc finger 4 and 5 from human INSM1, an essential regulator of neuroendocrine differentiation. Issue 5 (16th February 2017)

• Record Type: Journal Article
• Authors: Zhu, Jiang; Wang, Huapu; Ramelot, Theresa A.; Kennedy, Michael A.; Hu, Rui; Yue, Xiali; Liu, Maili; Yang, Yunhuang
• Is Part Of: Proteins. Volume 85:Issue 5(2017)
• Page Start: 957
• Page End: 962
• Publication Date: 2017-02-16
• Subjects: INSM1 -- ZF4‐5 -- consensus DNA -- solution structure -- mechanism; Proteins -- Periodicals; Proteins -- Periodicals; 572.6
• DOI: 10.1002/prot.25259
• Languages: English
• ISSNs: 0887-3585

Abstract

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.