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?

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 m...

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Bibliographic Details
Main Authors: Selene Gil-Moreno, Elena Jiménez-Martí, Òscar Palacios, Oliver Zerbe, Reinhard Dallinger, Mercè Capdevila, Sílvia Atrian
Format: Article
Language:English
Published: MDPI AG 2015-12-01
Series:International Journal of Molecular Sciences
Subjects:
Cd-isoform
domain linker sequence
Helix pomatia
metallothionein
metal binding
Online Access:http://www.mdpi.com/1422-0067/17/1/6

Internet

http://www.mdpi.com/1422-0067/17/1/6

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