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Solution structure of At3g04780.1‐des15, an Arabidopsis thaliana ortholog of the C‐terminal domain of human thioredoxin‐like protein
Author(s) -
Song Jikui,
Tyler Robert C.,
Wrobel Russell L.,
Frederick Ronnie O.,
Vojtek Frank C.,
Jeon Won Bae,
Lee Min S.,
Markley John L.
Publication year - 2005
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.041246805
Subject(s) - arabidopsis thaliana , barrel (horology) , thioredoxin , arabidopsis , protein structure , biology , nuclear magnetic resonance spectroscopy , c terminus , biophysics , chemistry , crystallography , amino acid , biochemistry , stereochemistry , gene , materials science , mutant , composite material
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.