Publication: Does Variation of the Inter-Domain Linker Sequence Modulate the Metal Binding Behaviour of Helix pomatia Cd-Metallothionein?
Does Variation of the Inter-Domain Linker Sequence Modulate the Metal Binding Behaviour of Helix pomatia Cd-Metallothionein?
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Gil-Moreno, S., Jiménez-Martí, E., Palacios, O., Zerbe, O., Dallinger, R., Capdevila, M., & Atrian, S. (2016). Does Variation of the Inter-Domain Linker Sequence Modulate the Metal Binding Behaviour of Helix pomatia Cd-Metallothionein? International Journal of Molecular Sciences, 17(6), 1–13. https://doi.org/10.3390/ijms17010006
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Snail metallothioneins (MTs) constitute an ideal model to study structure/function relationships in these metal-binding polypeptides. Helix pomatia harbours three MT isoforms: the highly specific CdMT and CuMT, and an unspecific Cd/CuMT, which represent paralogous proteins with extremely different metal binding preferences while sharing high sequence similarity. Preceding work allowed assessing that, although, the Cys residues are responsible for metal ion coordination, metal specificity or preference is achieved by diversification of
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- Gil-Moreno, Selene
- Jiménez-Martí, Elena
- Palacios, Oscar
- Zerbe, O
- Dallinger, Reinhard
- Capdevila, Merce
- Atrian, Silvia
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Citations
Gil-Moreno, S., Jiménez-Martí, E., Palacios, O., Zerbe, O., Dallinger, R., Capdevila, M., & Atrian, S. (2016). Does Variation of the Inter-Domain Linker Sequence Modulate the Metal Binding Behaviour of Helix pomatia Cd-Metallothionein? International Journal of Molecular Sciences, 17(6), 1–13. https://doi.org/10.3390/ijms17010006
