Three-dimensional structure of the lithostathine protofibril, a protein involved in Alzheimer's disease.

ABSTRACT: Neurodegenerative diseases are characterized by the presence of filamentous aggregates of proteins. We previously established that lithostathine is a protein overexpressed in the pre-clinical stages of Alzheimer's disease. Furthermore, it is present in the pathognomonic lesions associated with Alzheimer's disease. After self-proteolysis, the N-terminally truncated form of lithostathine leads to the formation of fibrillar aggregates. Here we observed using atomic force microscopy that these aggregates consisted of a network of protofibrils, each of which had a twisted appearance. Electron microscopy and image analysis showed that this twisted protofibril has a quadruple helical structure. Three-dimensional X-ray structural data and the results of biochemical experiments showed that when for

SUBMITTER: Gregoire C 

PROVIDER: S-EPMC125531 | biostudies-literature | 2001 Jul

REPOSITORIES: biostudies-literature