Expanding the diversity of chemical protein modification allows post-translational mimicry

Sander I. van Kasteren, Holger B. Kramer, Henrik H. Jensen, Sandra J. Campbell, Joanna Kirkpatrick, Neil J. Oldham, Daniel C. Anthony and Benjamin G. Davis
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Sander I. van Kasteren: University of Oxford, Chemistry Research Laboratory, Mansfield Road, Oxford OX1 3TA, UK
Holger B. Kramer: University of Oxford, Chemistry Research Laboratory, Mansfield Road, Oxford OX1 3TA, UK
Henrik H. Jensen: University of Oxford, Chemistry Research Laboratory, Mansfield Road, Oxford OX1 3TA, UK
Sandra J. Campbell: University of Oxford, Mansfield Road, Oxford OX1 3QT, UK
Joanna Kirkpatrick: University of Oxford, Chemistry Research Laboratory, Mansfield Road, Oxford OX1 3TA, UK
Neil J. Oldham: University of Oxford, Chemistry Research Laboratory, Mansfield Road, Oxford OX1 3TA, UK
Daniel C. Anthony: University of Oxford, Mansfield Road, Oxford OX1 3QT, UK
Benjamin G. Davis: University of Oxford, Chemistry Research Laboratory, Mansfield Road, Oxford OX1 3TA, UK

Nature, 2007, vol. 446, issue 7139, 1105-1109

Abstract: Many proteins are modulated by post-translational modifications, and it has generally not been possible to access pure mimics of complex post-translational modifications. Here, a chemical tagging method is used to attach multiple carbohydrates to bacterially expressed protein scaffolds, allowing reconstitution of functionally effective mimics of higher organism post-translational modifications.

Date: 2007
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DOI: 10.1038/nature05757

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