Tight complexes from disordered proteins

Berlow, Rebecca B.; Wright, Peter E.

doi:10.1038/d41586-018-01694-y

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21 February 2018

Tight complexes from disordered proteins

Charged groups on protein surfaces often take part in molecular interactions. Two unstructured proteins have been found to use charge complementarity to form a tight complex that has biologically useful kinetic properties.

Rebecca B. Berlow⁰ &
Peter E. Wright¹

Rebecca B. Berlow
1. Rebecca B. Berlow is in the Department of Integrative Structural and Computational Biology and The Skaggs Institute of Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, USA.
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Peter E. Wright
1. Peter E. Wright is in the Department of Integrative Structural and Computational Biology and The Skaggs Institute of Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, USA.
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The axiom ‘opposites attract’ applies to many aspects of life, including the many positively and negatively charged biological molecules that control the intricate cellular processes that enable an organism to survive. Even in the crowded environment of a cell, proteins can seek out their binding partners by using charged regions to attract oppositely charged molecules. This is certainly the case for the extreme example described in a paper in Nature by Borgia et al.¹, in which a high degree of opposing charge in two binding partners that lack a defined 3D structure enables the partners to associate rapidly to form a tight complex, without the need for specific interactions between amino-acid residues. Remarkably, the complex forms without either binding partner adopting a defined structure, thereby revealing a previously unknown interaction mechanism for biological molecules.

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Nature 555, 37-38 (2018)

doi: https://doi.org/10.1038/d41586-018-01694-y

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