Difference between revisions of "Part:BBa K3275001"
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=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>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.</ref>. Therefore, MTs are important for protecting the cell against heavy metal toxicity and maintaining cellular homeostasis. | ||
==Background== | ==Background== | ||
=Characterization= | =Characterization= | ||
=References= | =References= | ||
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. | 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. | ||
Revision as of 19:10, 24 September 2019
Cobalt Metallothionein
Oryctolagus cuniculus cobalt 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.
Background
Characterization
References
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.- ↑ 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.