1wou
From Proteopedia
(New page: 200px<br /> <applet load="1wou" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wou, resolution 1.8Å" /> '''Crystal Structure of...) |
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caption="1wou, resolution 1.8Å" /> | caption="1wou, resolution 1.8Å" /> | ||
'''Crystal Structure of human Trp14'''<br /> | '''Crystal Structure of human Trp14'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1WOU 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:// | + | 1WOU 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=1WOU 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 17:07:46 2008'' |
Revision as of 15:07, 15 February 2008
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Crystal Structure of human Trp14
Overview
Thioredoxin-related protein 14 (TRP14) is involved in regulating tumor, necrosis factor-alpha-induced signaling pathways in a different manner, from human thioredoxin 1 (Trx1). Here, we report the crystal structure of, human TRP14 determined at 1.8-A resolutions. The structure reveals a, typical thioredoxin fold with characteristic structural features that, account for the substrate specificity of the protein. The surface of TRP14, in the vicinity of the active site includes an extended loop and an, additional alpha-helix, and the distribution of charged residues in the, surface is different from Trx1. The distinctive dipeptide between the, redox-active cysteines contributes to stabilizing the thiolate anion of, the active site cysteine 43, increasing reactivity of the cysteine toward, substrates. These structural differences in the active site suggest that, TRP14 has evolved to regulate cellular redox signaling by recognizing a, distinctive group of substrates that would complement the group of, proteins regulated by Trx1.
About this Structure
1WOU is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis of cellular redox regulation by human TRP14., Woo JR, Kim SJ, Jeong W, Cho YH, Lee SC, Chung YJ, Rhee SG, Ryu SE, J Biol Chem. 2004 Nov 12;279(46):48120-5. Epub 2004 Sep 7. PMID:15355959
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