Difference between revisions of "Part:BBa K3275000"
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__TOC__ | __TOC__ | ||
=Introduction= | =Introduction= | ||
| + | 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 <ref>Ngu, T. and Stillman, M. (2006). Arsenic Binding to Human Metallothionein. Journal of the American Chemical Society, 128(38), pp.12473-12483.</ref>. Therefore, MTs are important for protecting the cell against heavy metal toxicity and maintaining cellular homeostasis. | ||
| + | ==Arsenic Metallothionein== | ||
==Background== | ==Background== | ||
=Characterization= | =Characterization= | ||
=References= | =References= | ||
Ngu, T. and Stillman, M. (2006). Arsenic Binding to Human Metallothionein. Journal of the American Chemical Society, 128(38), pp.12473-12483. | Ngu, T. and Stillman, M. (2006). Arsenic Binding to Human Metallothionein. Journal of the American Chemical Society, 128(38), pp.12473-12483. | ||
Revision as of 19:13, 24 September 2019
Arsenic metallothionein
Human arsenic targeting metallothionein
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BamHI site found at 3
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Introduction
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.
Arsenic Metallothionein
Background
Characterization
References
Ngu, T. and Stillman, M. (2006). Arsenic Binding to Human Metallothionein. Journal of the American Chemical Society, 128(38), pp.12473-12483.- ↑ Ngu, T. and Stillman, M. (2006). Arsenic Binding to Human Metallothionein. Journal of the American Chemical Society, 128(38), pp.12473-12483.