期刊
PROTEIN SCIENCE
卷 14, 期 4, 页码 1059-1063出版社
WILEY
DOI: 10.1110/ps.041246805
关键词
structural genomics; Arabidopsis thaliana; NMR; TXNL_HUMAN ortholog
资金
- NCRR NIH HHS [P41 RR 02301, S10 RR002781, P41 RR002301, S10 RR008438, RR 02781, RR 08438] Funding Source: Medline
- NIGMS NIH HHS [P41 GM 66326, P41 GM066326, P50 GM064598, 1P50 GM 64598] Funding Source: Medline
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-des 15 provides an entry point for understanding its functional role and those of its mammalian homologs.
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