Thioredoxin: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<StructureSection load="1ert" size="400" side="right" caption="Human thioredoxin (PDB entry 1ERT)"> | |||
<script> | |||
stage.loadFile("rcsb://1ert", {defaultRepresentation: true}).then(function(o){ | |||
// Remove a representação padrão | |||
o.removeAllRepresentations(); | |||
// Colorir hélices α de vermelho | |||
o.addRepresentation("cartoon", { | |||
sele: "helix", | |||
color: "red" | |||
}); | |||
// Colorir folhas β de azul | |||
o.addRepresentation("cartoon", { | |||
sele: "sheet", | |||
color: "blue" | |||
}); | |||
// Exibir o restante da proteína em cinza claro | |||
o.addRepresentation("cartoon", { | |||
sele: "protein and not (helix or sheet)", | |||
color: "lightgrey" | |||
}); | |||
stage.autoView(); | |||
}); | |||
</script> | |||
</StructureSection> | |||
<p> | |||
All thioredoxin proteins share a common structure, consisting of <b>four α-helices</b> (highlighted in red) and <b>five β-sheets</b> (highlighted in blue). This conserved fold is crucial for the redox activity of thioredoxins. | |||
</p> | |||
The <scene name='43/430885/Cv/4'>active site motif Cys-Gly-Pro-Cys</scene> is involved in the reduction of disulfide bonds in proteins<ref>Åslund F et al. (1997). J Biol Chem. 272(48):30780–30786.</ref>. | The <scene name='43/430885/Cv/4'>active site motif Cys-Gly-Pro-Cys</scene> is involved in the reduction of disulfide bonds in proteins<ref>Åslund F et al. (1997). J Biol Chem. 272(48):30780–30786.</ref>. | ||
Unlike many other thioredoxins, the human cytoplasmic thioredoxin has three cysteine residues (Cys 62, Cys 69, Cys 73) additional to the active site <scene name='43/430885/Cv/2'>Cys 32 and Cys 35</scene>. | Unlike many other thioredoxins, the human cytoplasmic thioredoxin has three cysteine residues (Cys 62, Cys 69, Cys 73) additional to the active site <scene name='43/430885/Cv/2'>Cys 32 and Cys 35</scene>. | ||
