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- Title
The N-terminus of mature human frataxin is intrinsically unfolded.
- Authors
Prischi, Filippo; Giannini, Clelia; Adinolfi, Salvatore; Pastore, Annalisa
- Abstract
Frataxin is a highly conserved nuclear-encoded mitochondrial protein whose deficiency is the primary cause of Friedreich's ataxia, an autosomal recessive neurodegenerative disease. The frataxin structure comprises a well-characterized globular domain that is present in all species and is preceded in eukaryotes by a non-conserved N-terminal tail that contains the mitochondrial import signal. Little is known about the structure and dynamic properties of the N-terminal tail. Here, we show that this region is flexible and intrinsically unfolded in human frataxin. It does not alter the iron-binding or self-aggregation properties of the globular domain. It is therefore very unlikely that this region could be important for the conserved functions of the protein.
- Publication
The FEBS journal, 2009, Vol 276, Issue 22, p6669
- ISSN
1742-4658
- Publication type
Journal Article
- DOI
10.1111/j.1742-4658.2009.07381.x