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| Line 40: |
Line 40: |
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| == Structural highlights == | | == Structural highlights == |
| <StructureSection load="1ert" size="400" side="right" caption="Human thioredoxin (PDB entry 1ERT)">
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| <script>
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| stage.loadFile("rcsb://1ert", {defaultRepresentation: true}).then(function(o){
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|
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| // Remove a representação padrão
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| o.removeAllRepresentations();
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|
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| // Colorir hélices α de vermelho
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| o.addRepresentation("cartoon", {
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| sele: "helix",
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| color: "red"
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| });
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|
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| // Colorir folhas β de azul
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| o.addRepresentation("cartoon", {
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| sele: "sheet",
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| color: "blue"
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| });
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|
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| // Exibir o restante da proteína em cinza claro
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| o.addRepresentation("cartoon", {
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| sele: "protein and not (helix or sheet)",
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| color: "lightgrey"
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| });
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|
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| stage.autoView();
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| });
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| </script>
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| </StructureSection>
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|
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| <p>
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| 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.
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| </p>
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|
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| 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>. |
