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Ionic self-complementarity induces amyloid-like fibril formation in an isolated domain of a plant copper metallochaperone protein |
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| Authors: | Helena?Mira Mar?al?Vilar Vicent?Esteve Marc?Martinell Marcelo?J?Kogan Ernest?Giralt David?Salom Ismael?Mingarro Lola?Pe?arrubia |
| Institution: | 1.Departament de Bioquímica i Biologia Molecular,Universitat de València,Burjassot,Spain;2.Institut de Recerca Biomèdica de Barcelona (IRBB-PCB),Universitat de Barcelona,Barcelona,Spain;3.Departament de Química Orgànica,Universitat de Barcelona,Barcelona,Spain;4.Department of Biochemistry and Biophysics,University of Pennsylvania,Philadelphia,USA;5.Fundación Valenciana de Investigaciones Biomédicas, CSIC,València,Spain;6.Novasite Pharmaceuticals,San Diego,USA |
| Abstract: | BackgroundArabidopsis thaliana copper metallochaperone CCH is a functional homologue of yeast antioxidant ATX1, involved in cytosolic copper transport. In higher plants, CCH has to be transported to specialised cells through plasmodesmata, being the only metallochaperone reported to date that leaves the cell where it is synthesised. CCH has two different domains, the N-terminal domain conserved among other copper-metallochaperones and a C-terminal domain absent in all the identified non-plant metallochaperones. The aim of the present study was the biochemical and biophysical characterisation of the C-terminal domain of the copper metallochaperone CCH. |
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