2iwt | pdb_00002iwt
THIOREDOXIN H2 (HVTRXH2) IN A MIXED DISULFIDE COMPLEX WITH THE TARGET PROTEIN BASI
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Overview
Thioredoxin is ubiquitous and regulates various target proteins through, disulfide bond reduction. We report the structure of thioredoxin (HvTrxh2, from barley) in a reaction intermediate complex with a protein substrate, barley alpha-amylase/subtilisin inhibitor (BASI). The crystal structure of, this mixed disulfide shows a conserved hydrophobic motif in thioredoxin, interacting with a sequence of residues from BASI through van der Waals, contacts and backbone-backbone hydrogen bonds. The observed structural, complementarity suggests that the recognition of features around protein, disulfides plays a major role in the specificity and protein disulfide, reductase activity of thioredoxin. This novel insight into the function of, thioredoxin constitutes a basis for comprehensive ... [(full description)]
About this Structure
2IWT is a [Protein complex] structure of sequences from [Hordeum vulgare] with FLC as [ligand]. Full crystallographic information is available from [OCA].
Reference
Structural basis for target protein recognition by the protein disulfide reductase thioredoxin., Maeda K, Hagglund P, Finnie C, Svensson B, Henriksen A, Structure. 2006 Nov;14(11):1701-10. PMID:17098195
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