版权说明 操作指南
首页 > 成果 > 详情

Structural basis for specific DNA sequence recognition by the transcription factor NFIL3

认领
导出
Link by DOI
反馈
分享
QQ微信 微博
成果类型:
期刊论文
作者:
Chen, Sizhuo;Lei, Ming;Liu, Ke*;Min, Jinrong*
通讯作者:
Liu, Ke;Min, Jinrong
作者机构:
[Chen, Sizhuo; Lei, Ming] Hubei Key Laboratory of Genetic Regulation and Integrative Biology, School of Life Sciences, Central China Normal University, Wuhan 430079, PR China
[Liu, Ke] Hubei Key Laboratory of Genetic Regulation and Integrative Biology, School of Life Sciences, Central China Normal University, Wuhan 430079, PR China. Electronic address: keliu2015@ccnu.edu.cn
[Min, Jinrong] Hubei Key Laboratory of Genetic Regulation and Integrative Biology, School of Life Sciences, Central China Normal University, Wuhan 430079, PR China. Electronic address: minjinrong@ccnu.edu.cn
通讯机构:
[Liu, Ke; Min, Jinrong] H
Hubei Key Laboratory of Genetic Regulation and Integrative Biology, School of Life Sciences, Central China Normal University, Wuhan 430079, PR China. Electronic address:
语种:
英文
关键词:
C/EBP-related protein;DNA crystal structure;NFIL3;bZIP domain;disease-associated mutants
期刊:
Journal of Biological Chemistry
ISSN:
0021-9258
年:
2024
卷:
300
期:
3
页码:
105776
机构署名:
本校为第一且通讯机构
院系归属:
生命科学学院
摘要:
The CCAAT/enhancer-binding proteins (C/EBPs) constitute a family of pivotal transcription factors involved in tissue development, cellular function, proliferation, and differentiation. NFIL3, as one of them, plays an important role in regulating immune cell differentiation, circadian clock system and neural regeneration, yet its specific DNA recognition mechanism remains enigmatic. In this study, we showed by the ITC binding experiments that NFIL3 prefers to bind to the TTACGTAA DNA motif. Our structural studies revealed that the α-helical NFI...

反馈

验证码:
看不清楚,换一个
确定
取消

成果认领

标题:
用户 作者 通讯作者
请选择
请选择
确定
取消

提示

该栏目需要登录且有访问权限才可以访问

如果您有访问权限,请直接 登录访问

如果您没有访问权限,请联系管理员申请开通

管理员联系邮箱:yun@hnwdkj.com