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Structural biology

The twist in Crk signaling revealed

Nature Chemical Biology volume 7, pages 5–6 (2011)Cite this article

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Structures of 'on' and 'off' states of Crk reveal how prolyl cis-trans isomerization functions as a molecular switch in this key adaptor protein. Additionally, these structures show how an SH3 domain utilizes a noncanonical binding surface for self-regulation.

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Figure 1: Regulation of Crk function by a prolyl cis-trans isomerization switch and implications for connecting different signaling pathways in the cell.

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  1. Linda K. Nicholson and Soumya De are in the Department of Molecular Biology and Genetics, Cornell University, Ithaca, New York, USA.,

    Linda K Nicholson & Soumya De

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  1. Linda K Nicholson
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  2. Soumya De
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Correspondence to Linda K Nicholson.

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Nicholson, L., De, S. The twist in Crk signaling revealed. Nat Chem Biol 7, 5–6 (2011). https://doi.org/10.1038/nchembio.504

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