The C2 domain of PKCdelta is a phosphotyrosine binding domain

Article Abstract:

A study finds that the C2 domain of PKCdelta directly binds to phosphotyrosine peptides in a sequence-specific manner. The crystal structure of the PKCdelta C2 domain in complex with an optimal phosphopeptide shows a new mode of phosphotyrosine binding in which the phosphotyrosine moiety forms a ring-stacking interaction with a histidine residue of the C2 domain.

Carbon, Phosphoproteins, Tyrosine

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MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks

Article Abstract:

The mammalian MDC1/NFBD1 directly binds to phospho-H2AX (gamma H2AX) by specifically interacting with the phosphoepitope at the (gamma)H2AX carboxyl terminus. Through a combination of biochemical, cell-biological and X-ray crystallographic approaches, the molecular details of the MDC1/NFBD1-(gamma)H2AX complex are revealed.

Analysis, Genetic regulation, Phosphorylation, Genetic research

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