Thioredoxin: Difference between revisions

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 == Structural highlights ==
-The <scene name='43/430885/Cv/5'>active site motif Cys-Gly-Pro-Cys</scene> is involved in the reduction of disulfide bonds.
+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 thioredoxin has additional cysteines, including <scene name='43/430885/Cv/6'>Cys 73</scene>, which forms an intermolecular disulfide bridge in the homodimeric structure.
+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>.
+The human cytoplasmic thioredoxin crystal structure reveals a homodimer with <scene name='43/430885/Cv/2'>Cys 73 forming an intermolecular disulfide bridge</scene>
 == 3D Structures of Thioredoxin ==

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