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Structural basis of cellular redox regulation by human TRP14

Title
Structural basis of cellular redox regulation by human TRP14
Authors
Joo R.W.Seung J.K.Jeong W.Yoon H.C.Sang C.L.Yong J.C.Sue G.R.Seong E.R.
Ewha Authors
이서구정우진
SCOPUS Author ID
이서구scopusscopus; 정우진scopus
Issue Date
2004
Journal Title
Journal of Biological Chemistry
ISSN
0021-9258JCR Link
Citation
Journal of Biological Chemistry vol. 279, no. 46, pp. 48120 - 48125
Indexed
SCI; SCIE; SCOPUS WOS scopus
Document Type
Article
Abstract
Thioredoxin-related protein 14 (TRP 14) is involved in regulating tumor necrosis factor-α-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-Å 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 α-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.
DOI
10.1074/jbc.M407079200
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일반대학원 > 생명·약학부 > Journal papers
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