Abstract
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 β-barrel sandwich. A two-stranded anti-parallel β-sheet, which seals off one end of the β-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 β-barrel. The three-dimensional structure of At3g04780.1-des15 provides an entry point for understanding its functional role and those of its mammalian homologs.
Original language | English |
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Pages (from-to) | 1059-1063 |
Number of pages | 5 |
Journal | Protein Science |
Volume | 14 |
Issue number | 4 |
DOIs | |
State | Published - Apr 2005 |
Keywords
- Arabidopsis thaliana
- NMR
- Structural genomics
- TXNL_HUMAN ortholog