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

Hsin-Hui Wu | Zendy; PeiYu Wu | Zendy; Kai-Fa Huang | Zendy; Yu-Ya Kao | Zendy; MingDaw Tsai | Zendy

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

Author(s) -

Hsin-Hui Wu,

PeiYu Wu,

Kai-Fa Huang,

Yu-Ya Kao,

MingDaw Tsai

Publication year - 2012

Publication title -

biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.43

H-Index - 253

eISSN - 1520-4995

pISSN - 0006-2960

DOI - 10.1021/bi201709w

Subject(s) - dimer , ligand (biochemistry) , dna , microbiology and biotechnology , biophysics , chemistry , biology , biochemistry , receptor , organic chemistry

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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