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On the supertertiary structure of proteins

Nature Chemical Biology volume 8, pages 597–600 (2012)Cite this article

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Intrinsically disordered proteins and complex multidomain proteins are characterized by a dynamic ensemble of conformations that cannot be unequivocally described by traditional static terms of structural biology. The functional importance of this structural complexity necessitates new standards and protocols for the description and deposition of such 'supertertiary' structural ensembles into structural databases.

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Figure 1: Heterogeneity of supertertiary structures in three multidomain proteins.
Figure 2: Conformational energy landscape of tertiary and supertertiary structures.

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Acknowledgements

This work was supported by the Research Foundation Flanders (FWO) Odysseus grant G.0029.12. The author is grateful to A. Bekesi for helpful discussions and to S. Kosol for her help in preparing the figures.

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  1. Peter Tompa is at the VIB Department of Structural Biology, Vrije Universiteit Brussel, Brussels, Belgium and the Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary.,

    Peter Tompa

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Tompa, P. On the supertertiary structure of proteins. Nat Chem Biol 8, 597–600 (2012). https://doi.org/10.1038/nchembio.1009

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