Song Jikui, Tyler Robert C, Wrobel Russell L, Frederick Ronnie O, Vojtek Frank C, Jeon Won Bae, Lee Min S, Markley John L
Center for Eukaryotic Structural Genomics, Department of Biochemistry, 433 Babcock Drive, University of Wisconsin-Madison, Madison, WI 53706-1544, USA.
Protein Sci. 2005 Apr;14(4):1059-63. doi: 10.1110/ps.041246805. Epub 2005 Mar 1.
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.
通过核磁共振光谱法确定了拟南芥At3g04780.1-des15的结构,它是人类硫氧还蛋白样蛋白C端结构域的直系同源物。该结构主要由一个β-桶状三明治构成。一个由两条链组成的反平行β-折叠封闭了β-桶的一端,两侧是富含酸性氨基酸的两个柔性环。尽管这种折叠结构通常会提供一个配体结合位点,但该结构在β-桶内部并未显示出明显的腔。At3g04780.1-des15的三维结构为理解其功能作用及其哺乳动物同源物的功能作用提供了一个切入点。