Revision as of 19:15, 24 September 2019

Cobalt Metallothionein

Oryctolagus cuniculus cobalt targeting metallothionein.

Sequence and Features

Introduction

Background

Metallothionein (MT) is a class of small metal-binding proteins that exists in bacteria, plants and animals. These proteins depending on their amino acid compositions have a high binding affinity with different bivalent metal ions. Once MT detects the corresponding metal, it binds the goal through covalent bonds, which are composed of sulfhydryl cysteine residues and stores the metal by tightly chelating the metal. Typically, it is assumed that MTs have two binding domains, one of which is the C-terminal part (α-domain) with three binding sites. The other one is the N-terminal part (β-domain) with four divalent binding sites ^[1]. Therefore, MTs are important for protecting the cell against heavy metal toxicity and maintaining cellular homeostasis.

Cobalt Metallothionein

Characterization

References

1. ↑ Vasak, M. and Kagi, J. (1981). Metal thiolate clusters in cobalt(II)-metallothionein. Proceedings of the National Academy of Sciences, 78(11), pp.6709-6713.