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Phosphothreonine recognition comes into focus

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The structure of the Rad53p FHA domain reveals a new fundamental mechanism governing phosphothreonine-dependent protein–protein interactions in nuclear processes including DNA repair and replication in a broad range of organisms.

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Figure 1: Ribbon diagram of the Rad53p FHA1 domain in complex with a phosphothreonine peptide derived from Rad9p.
Figure 2: Molecular basis of phosphothreonine recognition by the FHA1 domain.

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Acknowledgements

I thank S.P. Jackson and S.J. Smerdon for providing the FHA1 domain coordinates, and A. Farooq and K.S. Yan for helping with figure preparation and discussion.

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  1. the Department of Physiology and Biophysics, Structural Biology Program, Mount Sinai School of Medicine, New York University, 1425 Madison Avenue, Box 1677, New York, 10029, New York, USA

    Ming-Ming Zhou

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Zhou, MM. Phosphothreonine recognition comes into focus. Nat Struct Mol Biol 7, 1085–1087 (2000). https://doi.org/10.1038/81919

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