The centriolar protein CPAP G-box: an amyloid fibril in a single domain: 5

Centrioles are evolutionarily conserved cylindrical cell organelleswith characteristic radial symmetry. Despite their considerable size (400 nm x 200 nm, in humans), genetic studies suggest that relatively few protein components are involved in their assembly. We recently characterized the molecular architecture of the centrosomal P4.1-associated protein (CPAP), which is crucial for controlling the centriolar cylinder length. Here, we review the remarkable architecture of the C-terminal domain of CPAP, termed the G-box, which comprises a single, entirely solvent exposed, antiparallel beta-sheet. Molecular dynamics simulations support the stability of the G-box domain even in the face of truncations or amino acid substitutions. The similarity of the G-box domain to amyloids (or amyloid precursors) is strengthened by its oligomeric arrangement to form continuous fibrils. G-box fibrils were observed in crystals as well as in solution and are also supported by simulations. We conclude that the G-box domain may well represent the best analogue currently available for studies of exposed beta-sheets, unencumbered by additional structural elements or severe aggregations problems.

Published in:
Biochemical Society Transactions, 43, 838-843
London, Portland Press Ltd

 Record created 2015-12-02, last modified 2018-03-17

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