Prischi, Filippo and Giannini, Clelia and Adinolfi, Salvatore and Pastore, Annalisa (2009) 'The N-terminus of mature human frataxin is intrinsically unfolded.' FEBS Journal, 276 (22). pp. 6669-6676. ISSN 1742-464X

Preview

Text Prischi_et_al-2009-FEBS_Journal.pdf - Published Version Download (2MB) | Preview

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
Uncontrolled Keywords:	dynamics; Friedreich's ataxia; IUPs; NMR; structure
Subjects:	Q Science > Q Science (General)
Divisions:	Faculty of Science and Health Faculty of Science and Health > Life Sciences, School of
SWORD Depositor:	Elements
Depositing User:	Elements
Date Deposited:	04 Feb 2016 11:44
Last Modified:	18 Aug 2022 11:31
URI:	http://repository.essex.ac.uk/id/eprint/14829

Actions (login required)

View Item