Structural basis of cellular redox regulation by human TRP14

Cited 32 time in scopus
Metadata Downloads
Structural basis of cellular redox regulation by human TRP14
Joo Rang Woo; Seung-Jun Kim; W Jeong; Yoon Hea Cho; Sang Chul Lee; Y J Chung; S G Rhee; Seong Eon Ryu
Bibliographic Citation
Journal of Biological Chemistry, vol. 279, no. 46, pp. 48120-48125
Publication Year
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.
Amer Soc Biochemistry Molecular Biology Inc
Appears in Collections:
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.

Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.