| Literature DB >> 15741346 |
Jikui Song1, Robert C Tyler, Russell L Wrobel, Ronnie O Frederick, Frank C Vojtek, Won Bae Jeon, Min S Lee, John L Markley.
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 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-des15 provides an entry point for understanding its functional role and those of its mammalian homologs.Entities:
Mesh:
Substances:
Year: 2005 PMID: 15741346 PMCID: PMC2253455 DOI: 10.1110/ps.041246805
Source DB: PubMed Journal: Protein Sci ISSN: 0961-8368 Impact factor: 6.725