3VA4

Crystal structure of the mammalian MDC1 FHA domain complexed with CHK2 pThr68 peptide

Summary for 3VA4

• Entry DOI: 10.2210/pdb3va4/pdb
• Related: 3VA1
• Descriptor: Mediator of DNA damage checkpoint protein 1, Serine/threonine-protein kinase Chk2 (3 entities in total)
• Functional Keywords: cell cycle, fha domain, dna-damage, chk2 and mdc1 dimerization
• Biological source: Mus musculus; More
• Cellular location: Nucleus: Q5PSV9; Isoform 2: Nucleus. Isoform 4: Nucleus. Isoform 7: Nucleus. Isoform 9: Nucleus. Isoform 12: Nucleus. Nucleus, PML body: O96017
• Total number of polymer chains: 3
• Total formula weight: 30528.76

Authors

Wu, H.H.,Wu, P.Y.,Huang, K.F.,Kao, Y.Y.,Tsai, M.D. (deposition date: 2011-12-28, release date: 2012-02-01, Last modification date: 2024-10-09)

Primary citation

Wu, H.H.,Wu, P.Y.,Huang, K.F.,Kao, Y.Y.,Tsai, M.D.
Structural Delineation of MDC1-FHA Domain Binding with CHK2-pThr68.
Biochemistry, 2012

PubMed 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.

PubMed: 22211259
DOI: 10.1021/bi201709w

Experimental method

X-RAY DIFFRACTION (1.54 Å)