2iwt

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[[Image:2iwt.jpg|left|200px]]
[[Image:2iwt.jpg|left|200px]]
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{{Structure
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{{STRUCTURE_2iwt| PDB=2iwt | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2iwt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iwt OCA], [http://www.ebi.ac.uk/pdbsum/2iwt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2iwt RCSB]</span>
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'''THIOREDOXIN H2 (HVTRXH2) IN A MIXED DISULFIDE COMPLEX WITH THE TARGET PROTEIN BASI'''
'''THIOREDOXIN H2 (HVTRXH2) IN A MIXED DISULFIDE COMPLEX WITH THE TARGET PROTEIN BASI'''
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[[Category: Maeda, K.]]
[[Category: Maeda, K.]]
[[Category: Svensson, B.]]
[[Category: Svensson, B.]]
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[[Category: alpha-amylase inhibitor]]
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[[Category: Alpha-amylase inhibitor]]
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[[Category: amy2]]
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[[Category: Amy2]]
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[[Category: basi]]
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[[Category: Basi]]
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[[Category: disulfide intermediate]]
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[[Category: Disulfide intermediate]]
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[[Category: disulfide reductase]]
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[[Category: Disulfide reductase]]
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[[Category: oxidoreductase]]
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[[Category: Oxidoreductase]]
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[[Category: protease inhibitor]]
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[[Category: Protease inhibitor]]
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[[Category: redox]]
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[[Category: Redox]]
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[[Category: serine protease inhibitor]]
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[[Category: Serine protease inhibitor]]
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[[Category: substrate recognition]]
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[[Category: Substrate recognition]]
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[[Category: thioredoxin]]
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[[Category: Thioredoxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:00:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:49:46 2008''
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Revision as of 05:00, 4 May 2008

Template:STRUCTURE 2iwt

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 understanding of its biological role. Moreover, comparison with structurally related proteins shows that thioredoxin shares a mechanism with glutaredoxin and glutathione transferase for correctly positioning substrate cysteine residues at the catalytic groups but possesses a unique structural element that allows recognition of protein disulfides.

About this Structure

2IWT is a Protein complex structure of sequences from Hordeum vulgare. 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 Sun May 4 08:00:29 2008

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