2iwt
From Proteopedia
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THIOREDOXIN H2 (HVTRXH2) IN A MIXED DISULFIDE COMPLEX WITH THE TARGET PROTEIN BASI
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]. Structure known Active Site: AC1. 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
Page seeded by OCA on Tue Oct 30 17:17:59 2007
Categories: Hordeum vulgare | Protein complex | Finnie, C. | Hagglund, P. | Henriksen, A. | Maeda, K. | Svensson, B. | FLC | Alpha-amylase inhibitor | Amy2 | Basi | Disulfide intermediate | Disulfide reductase | Oxidoreductase | Protease inhibitor | Redox | Serine protease inhibitor | Substrate recognition | Thioredoxin
