Truncation of alphaB-crystallin by the myopathy-causing Q151X mutation significantly destabilizes the protein leading to aggregate formation in transfected cells.

Abstract excerpt

Here we investigate the effects of a myopathy-causing mutation in alphaB-crystallin, Q151X, upon its structure and function. This mutation removes the C-terminal domain of alphaB-crystallin, which is expected to compromise both its oligomerization and chaperone activity. We compared this to two other alphaB-crystallin mutants (450delA, 464delCT) and also to a series of C-terminal truncations (E164X, E165X, K174X,...

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