Amyloid formation by human carboxypeptidase D transthyretin-like domain under physiological conditions.

ABSTRACT: Protein aggregation is linked to a growing list of diseases, but it is also an intrinsic property of polypeptides, because the formation of functional globular proteins comes at the expense of an inherent aggregation propensity. Certain proteins can access aggregation-prone states from native-like conformations without the need to cross the energy barrier for unfolding. This is the case of transthyretin (TTR), a homotetrameric protein whose dissociation into its monomers initiates the aggregation cascade. Domains with structural homology to TTR exist in a number of proteins, including the M14B subfamily carboxypeptidases. We show here that the monomeric transthyretin-like domain of human carboxypeptidase D aggregates under close to physiological conditions into amyloid structures, with the

SUBMITTER: Garcia-Pardo J 

PROVIDER: S-EPMC4256313 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature