Crystal structure and mutation analysis revealed that DREP2 CIDE forms a filament-like structure with features differing from those of DREP4 CIDE

被引：6

作者：

Ha, Hyun Ji ^{[1
]}

Park, Hyun Ho ^{[1
]}

机构：

[1] Chung Ang Univ, Coll Pharm, Seoul 06974, South Korea

来源：

SCIENTIFIC REPORTS | 2018年 / 8卷

基金：

新加坡国家研究基金会;

关键词：

CASPASE-ACTIVATED DNASE; FRAGMENTATION SYSTEM; N DOMAIN; INHIBITOR; APOPTOSIS; PROTEIN; NUCLEASE; COMPLEX; MODEL; IDENTIFICATION;

D O I：

10.1038/s41598-018-36253-y

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Cell death-inducing DFF45-like effect (CIDE) domain-containing proteins, DFF40, DFF45, CIDE-A, CIDE-B, and FSP27, play important roles in apoptotic DNA fragmentation and lipid homeostasis. The function of DFF40/45 in apoptotic DNA fragmentation is mediated by CIDE domain filament formation. Although our recent structural study of DREP4 CIDE revealed the first filament-like structure of the CIDE domain and its functional importance, the filament structure of DREP2 CIDE is unclear because this structure was not helical in the asymmetric unit. In this study, we present the crystal structure and mutagenesis analysis of the DREP2 CIDE mutant, which confirmed that DREP2 CIDE also forms a filament-like structure with features differing from those of DREP4 CIDE.

引用

页数：11

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