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Active site-directed protein regulation

Nature volume 402, pages 373–376 (1999)Cite this article

Abstract

Regulation of protein function is vital for the control of cellular processes. Proteins are often regulated by allosteric mechanisms, in which effectors bind to regulatory sites distinct from the active sites and alter protein function. Intrasteric regulation, directed at the active site and thus the counterpart of allosteric control, is now emerging as an important regulatory mechanism.

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Figure 1: Representation of intrasteric regulation.
Figure 2: Three-dimensional (3D) structures of representative proteins under intrasteric control through active site-directed autoregulatory sequences.

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Acknowledgements

We thank J. Heierhorst, I. Jennings and other members of the protein research groups at St. Vincent's Institute for discussions; T. Teh for comments on the manuscript; and P. Carr for unpublished data. The work was supported by the National Health and Medical Research Council, Wellcome Trust, Australian Research Council and National Heart Foundation; B.K. is a Wellcome Senior Research Fellow in Medical Science in Australia; B.E.K. is an NHMRC Fellow.

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  1. St. Vincent's Institute of Medical Research, 41 Victoria Parade, Fitzroy, 3065, Victoria, Australia

    Bostjan Kobe & Bruce E. Kemp

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Correspondence to Bostjan Kobe.

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Kobe, B., Kemp, B. Active site-directed protein regulation . Nature 402, 373–376 (1999). https://doi.org/10.1038/46478

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