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'''THE HIGH-RESOLUTION THREE-DIMENSIONAL SOLUTION STRUCTURES OF THE OXIDIZED AND REDUCED STATES OF HUMAN THIOREDOXIN''' | {{Structure | ||
|PDB= 1trw |SIZE=350|CAPTION= <scene name='initialview01'>1trw</scene> | |||
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'''THE HIGH-RESOLUTION THREE-DIMENSIONAL SOLUTION STRUCTURES OF THE OXIDIZED AND REDUCED STATES OF HUMAN THIOREDOXIN''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1TRW is a [ | 1TRW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TRW OCA]. | ||
==Reference== | ==Reference== | ||
The high-resolution three-dimensional solution structures of the oxidized and reduced states of human thioredoxin., Qin J, Clore GM, Gronenborn AM, Structure. 1994 Jun 15;2(6):503-22. PMID:[http:// | The high-resolution three-dimensional solution structures of the oxidized and reduced states of human thioredoxin., Qin J, Clore GM, Gronenborn AM, Structure. 1994 Jun 15;2(6):503-22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7922028 7922028] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: electron transport]] | [[Category: electron transport]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:22:28 2008'' | ||
Revision as of 15:22, 20 March 2008
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THE HIGH-RESOLUTION THREE-DIMENSIONAL SOLUTION STRUCTURES OF THE OXIDIZED AND REDUCED STATES OF HUMAN THIOREDOXIN
OverviewOverview
BACKGROUND: Thioredoxin is a ubiquitous protein and is involved in a variety of fundamental biological functions. Its active site is conserved and has two redox active cysteines in the sequence Trp-Cys-Gly-Pro-Cys. No structures of the oxidized and reduced states from the same species have been determined at high resolution under the same conditions and using the same methods. Hence, any detailed comparison of the two oxidation states has been previously precluded. RESULTS: The reduced and oxidized states of the (C62A, C69A, C73A) mutant of human thioredoxin have been investigated by multidimensional heteronuclear NMR. Structures for both states were determined on the basis of approximately 28 experimental restraints per residue, and the resulting precision of the two structures is very high. Consequently, subtle differences between the oxidized and reduced states can be reliably assessed and evaluated. Small differences, particularly within and around the active site can be discerned. CONCLUSIONS: Overall, the structures of the reduced and oxidized states of the (C62A, C69A, C73A) mutant of human thioredoxin are very similar (with a backbone atomic root mean square difference of about 0.9 A) and the packing of side chains within the protein core is nearly identical. The conformational change between oxidized and reduced human thioredoxin is very small and localized to areas in spatial proximity to the redox active cysteines. These subtle structural differences, in addition to the restriction of conformational freedom within the active site upon oxidation, may be important for the different activities of thioredoxin involving a variety of target proteins.
DiseaseDisease
Known disease associated with this structure: Ciliary dyskinesia, primary, 6 OMIM:[607421]
About this StructureAbout this Structure
1TRW is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
The high-resolution three-dimensional solution structures of the oxidized and reduced states of human thioredoxin., Qin J, Clore GM, Gronenborn AM, Structure. 1994 Jun 15;2(6):503-22. PMID:7922028
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