Literature DB >> 22211259

Structural delineation of MDC1-FHA domain binding with CHK2-pThr68.

Hsin-Hui Wu1, Pei-Yu Wu, Kai-Fa Huang, Yu-Ya Kao, Ming-Daw Tsai.   

Abstract

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.

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Year:  2012        PMID： 22211259     DOI： 10.1021/bi201709w

Source DB:  PubMed          Journal:  Biochemistry        ISSN： 0006-2960            Impact factor:   3.162


  8 in total

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