Difference between revisions of "Part:BBa K3275000"
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=Introduction=
 
=Introduction=
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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.
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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> Ruttkay-Nedecky, B., Nejdl, L., Gumulec, J., Zitka, O., Masarik, M., Eckschlager, T., . . . Kizek, R. (2013, March 15). The role of metallothionein in oxidative stress. Retrieved from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3634463/</ref>. Therefore, MTs are important for protecting the cell against heavy metal toxicity and maintaining cellular homeostasis.
 
==Arsenic Metallothionein==
 
==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.

Revision as of 01:57, 3 October 2019


Arsenic metallothionein

Human arsenic targeting metallothionein

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BamHI site found at 3
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE 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.
  1. ↑ Ruttkay-Nedecky, B., Nejdl, L., Gumulec, J., Zitka, O., Masarik, M., Eckschlager, T., . . . Kizek, R. (2013, March 15). The role of metallothionein in oxidative stress. Retrieved from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3634463/