1trv: Difference between revisions
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'''THE HIGH-RESOLUTION THREE-DIMENSIONAL SOLUTION STRUCTURES OF THE OXIDIZED AND REDUCED STATES OF HUMAN THIOREDOXIN'''<br /> | '''THE HIGH-RESOLUTION THREE-DIMENSIONAL SOLUTION STRUCTURES OF THE OXIDIZED AND REDUCED STATES OF HUMAN THIOREDOXIN'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1TRV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 1TRV is a [http://en.wikipedia.org/wiki/Single_protein 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=1TRV OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: electron transport]] | [[Category: electron transport]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:58:13 2008'' | ||
Revision as of 17:58, 15 February 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
1TRV 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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