Solution structure of At3g04780.1-des15, an Arabidopsis thaliana ortholog of the C-terminal domain of human thioredoxin-like protein

Jikui Song, Robert C. Tyler, Russell L. Wrobel, Ronnie O. Frederick, Frank C. Vojtek, Won Bae Jeon, Min S. Lee, John L. Markley

Research output: Contribution to journalArticlepeer-review

11 Scopus citations

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 languageEnglish
Pages (from-to)1059-1063
Number of pages5
JournalProtein Science
Volume14
Issue number4
DOIs
StatePublished - Apr 2005

Keywords

  • Arabidopsis thaliana
  • NMR
  • Structural genomics
  • TXNL_HUMAN ortholog

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