Structural Delineation of MDC1-FHA Domain Binding with CHK2-pThr68

被引：10

作者：

Wu, Hsin-Hui ^{[1
,4
]}

Wu, Pei-Yu ^{[1
]}

Huang, Kai-Fa ^{[1
]}

Kao, Yu-Ya ^{[1
]}

Tsai, Ming-Daw ^{[1
,2
,3
,4
]}

机构：

[1] Acad Sinica, Inst Biol Chem, Taipei 115, Taiwan

[2] Acad Sinica, Genom Res Ctr, Taipei 115, Taiwan

[3] Natl Taiwan Univ, Inst Biochem Sci, Taipei 10617, Taiwan

[4] Natl Tsing Hua Univ, Inst Bioinformat & Struct Biol, Hsinchu 300, Taiwan

来源：

BIOCHEMISTRY | 2012年 / 51卷 / 02期

关键词：

DNA-DAMAGE RESPONSE; FHA DOMAIN; CHECKPOINT PROTEIN; COMPLEX; PHOSPHORYLATION; CHROMATIN; SITES; CHK2; NBS1; ATM;

D O I：

10.1021/bi201709w

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Mammalian MDC1 interacts with CHK2 in the regulation of DNA damage-induced S-phase checkpoint and apoptosis, which is directed by the association of MDC1-FHA and CHK2-pThr68. However, different ligand specificities of MDC1-FHA have been reported, and no structure is available. Here we report the crystal structures of MDC1-FHA and its complex with a CHK2 peptide containing pThr68. Unlike other FHA domains, MDC1-FHA exists as an intrinsic dimer in solution and in crystals. Structural and binding analyses support pThr+3 ligand specificity and provide structural insight into MDC1-CHK2 interaction.

引用

页码：575 / 577

页数：3

共 41 条

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