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Sculpting a domain by splicing

A recent study demonstrates that a short insert from alternative splicing in a common protein domain leads to rearrangements of surface loops and domain fold. The results provide a structural basis for the change of functional properties associated with alternative splicing.

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Figure 1: β-strand takeover by an alternatively spliced sequence.

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Acknowledgements

We thank J. Rizo for providing the atomic coordinates of the long C2A prior to publication.

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Davletov, B., Jiménez, J. Sculpting a domain by splicing. Nat Struct Mol Biol 11, 4–5 (2004). https://doi.org/10.1038/nsmb0104-4

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