Polyglutamine expansion affects huntingtin conformation in multiple Huntington's disease models.

ABSTRACT: Conformational changes in disease-associated or mutant proteins represent a key pathological aspect of Huntington's disease (HD) and other protein misfolding diseases. Using immunoassays and biophysical approaches, we and others have recently reported that polyglutamine expansion in purified or recombinantly expressed huntingtin (HTT) proteins affects their conformational properties in a manner dependent on both polyglutamine repeat length and temperature but independent of HTT protein fragment length. These findings are consistent with the HD mutation affecting structural aspects of the amino-terminal region of the protein, and support the concept that modulating mutant HTT conformation might provide novel therapeutic and diagnostic opportunities. We now report that the same conformationa

SUBMITTER: Daldin M 

PROVIDER: S-EPMC5505970 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature