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
收藏
页码：575 / 577
页数：3
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