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
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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 |
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| 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: | 15 Jan 2022 00:30 |
| URI: | http://repository.essex.ac.uk/id/eprint/14829 |
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