Thioredoxin: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
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>. | |||
The human cytoplasmic thioredoxin crystal structure reveals a homodimer with <scene name='43/430885/Cv/2'>Cys 73 forming an intermolecular disulfide bridge</scene>. | |||
<StructureSection load='1ert' size='350' side='right' caption='Human thioredoxin (PDB entry 1ERT)' scene='43/430885/Cv/2'/> | |||
<StructureSection load='1ert' size='350' side='right' caption='Human thioredoxin (PDB entry 1ERT)' scene='43/430885/Cv/ | |||
== 3D Structures of Thioredoxin == | == 3D Structures of Thioredoxin == | ||
