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Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/47500

Purification and characterization of Δ3Trx-1, a splicing variant of human thioredoxin-1 lacking exon 3

AutorJiménez, Alberto ; Miranda-Vizuete, Antonio
Palabras claveCytosol
Membrane proteins
Tumor cells
Fecha de publicación24-ene-2003
CitaciónProtein Expression and Purification 27(2): 319-324 (2003)
ResumenThioredoxins comprise a growing family of proteins that function as general protein-disulfide reductases and are maintained in their reduced active form by the flavoenzyme thioredoxin reductase. Human Trx-1 is mainly a cytosolic protein, although it has been shown to translocate into the nucleus upon certain stimuli and can also be secreted. We report here the expression and characterization of delta3Trx-1, a splicing variant of human Trx-1, lacking exon 3, which spans from residues 44 to 63 in the wild-type protein. Structure-based prediction of this splicing form indicates that delta3Trx-1 lacks helix alpha2 and strand beta3, which are implicated in substrate positioning and three-dimensional stabilization of the active site residues. Recombinant human delta3Trx-1 is recognized by polyclonal antibodies raised against full-length human Trx-1. However, delta3Trx-1 retains no enzymatic activity either with DTT or thioredoxin reductase and NADPH as reducing systems. Delta3Trx-1 competes with full-length Trx-1 for the interaction with thioredoxin reductase. The absence of helix alpha2 and strand beta3 in delta3Trx-1 is consistent with the lack of enzymatic activity and its potential dominant negative properties.
Descripción6 páginas, 5 figuras.
Versión del editorhttp://dx.doi.org/10.1016/S1046-5928(02)00607-1
ReferenciasPMID: 12597892
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