Journal
PROTEIN SCIENCE
Volume 14, Issue 4, Pages 1059-1063Publisher
WILEY
DOI: 10.1110/ps.041246805
Keywords
structural genomics; Arabidopsis thaliana; NMR; TXNL_HUMAN ortholog
Categories
Funding
- NCRR NIH HHS [P41 RR 02301, S10 RR002781, P41 RR002301, S10 RR008438, RR 02781, RR 08438] Funding Source: Medline
- NIGMS NIH HHS [P41 GM 66326, P41 GM066326, P50 GM064598, 1P50 GM 64598] Funding Source: Medline
Ask authors/readers for more resources
The structure of At3g04780.1-des15, an Arabidopsis thaliana ortholog of the C-terminal domain of human thioredoxin-like protein, was determined by NMR spectroscopy. The structure is dominated by a beta-barrel sandwich. A two-stranded anti-parallel beta-sheet, which seals off one end of the beta-barrel, is flanked by two flexible loops rich in acidic amino acids. Although this fold often provides a ligand binding site, the structure did not reveal an appreciable cavity inside the beta-barrel. The three-dimensional structure of At3g04780.1-des 15 provides an entry point for understanding its functional role and those of its mammalian homologs.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available