Prischi, F and Giannini, C and Adinolfi, S and Pastore, A (2009) 'The N-terminus of mature human frataxin is intrinsically unfolded.' FEBS Journal, 276 (22). 6669 - 6676. ISSN 1742-464X

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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. © 2009 FEBS.

Item Type:	Article
Subjects:	Q Science > Q Science (General)
Divisions:	Faculty of Science and Health > Life Sciences, School of
Depositing User:	Filippo Prischi
Date Deposited:	04 Feb 2016 11:44
Last Modified:	06 Sep 2019 17:15
URI:	http://repository.essex.ac.uk/id/eprint/14829

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