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Title 

Structural basis of cellular redox regulation by human TRP14

Authors 

Joo Rang WooSeung-Jun KimW JeongYoon Hea ChoSang Chul LeeY J ChungS G RheeSeong Eon Ryu

Publisher 

American Society for Biochemistry and Molecular Biology

Issue Date 

2004

Citation 

Journal of Biological Chemistry, vol. 279, no. 46, pp. 48120-48125

Keywords 

redox reactionscellular redox regulationshuman thioredoxin 1 (Trx1)human TRP14thioredoxinthioredoxin 1thioredoxin related protein 14humanhuman cellhumans

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-? 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.

ISSN 

0021-9258

Link 

http://dx.doi.org/10.1074/jbc.M407079200

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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