1wou
From Proteopedia
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| - | [[Image:1wou.jpg|left|200px]] | + | [[Image:1wou.jpg|left|200px]] |
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| - | '''Crystal Structure of human Trp14''' | + | {{Structure |
| + | |PDB= 1wou |SIZE=350|CAPTION= <scene name='initialview01'>1wou</scene>, resolution 1.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure of human Trp14''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1WOU is a [ | + | 1WOU 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=1WOU OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15355959 15355959] |
[[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 14:59:49 2008'' |
Revision as of 12:59, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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