Amyloid-like fibrils from a domain-swapping protein feature a parallel, in-register conformation without native-like interactions.

ABSTRACT: The formation of amyloid-like fibrils is characteristic of various diseases, but the underlying mechanism and the factors that determine whether, when, and how proteins form amyloid, remain uncertain. Certain mechanisms have been proposed based on the three-dimensional or runaway domain swapping, inspired by the fact that some proteins show an apparent correlation between the ability to form domain-swapped dimers and a tendency to form fibrillar aggregates. Intramolecular β-sheet contacts present in the monomeric state could constitute intermolecular β-sheets in the dimeric and fibrillar states. One example is an amyloid-forming mutant of the immunoglobulin binding domain B1 of streptococcal protein G, which in its native conformation consists of a four-stranded β-sheet and one α-helix. Un

SUBMITTER: Li J 

PROVIDER: S-EPMC3190706 | biostudies-literature | 2011 Aug

REPOSITORIES: biostudies-literature