Cooperative hydrophobic core interactions in the β-trefoil architecture.

Michael Blaber

Protein science : a publication of the Protein Society 2021 May

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Symmetric protein architectures have a compelling aesthetic that suggests a plausible evolutionary process (i.e., gene duplication/fusion) yielding complex architecture from a simpler structural motif. Furthermore, symmetry inspires a practical approach to computational protein design that substantially reduces the combinatorial explosion problem, and may provide practical solutions for structure optimization. Despite such broad relevance, the role of structural symmetry in the key area of hydrophobic core-packing cooperativity has not been adequately studied. In the present report, the threefold rotational symmetry intrinsic to the β-trefoil architecture is shown to form a geometric basis for highly-cooperative core-packing interactions that both stabilize the local repeating motif and promote oligomerization/long-range contacts in the folding process. Symmetry in the β-trefoil structure also permits tolerance towards mutational drift that involves a structural quasi-equivalence at several key core positions. © 2021 The Protein Society.

Citation

Michael Blaber. Cooperative hydrophobic core interactions in the β-trefoil architecture. Protein science : a publication of the Protein Society. 2021 May;30(5):956-965