Literature DB >> 15741346

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

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.

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Year:  2005        PMID: 15741346      PMCID: PMC2253455          DOI: 10.1110/ps.041246805

Source DB:  PubMed          Journal:  Protein Sci        ISSN: 0961-8368            Impact factor:   6.725


  19 in total

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7.  Torsion angle dynamics for NMR structure calculation with the new program DYANA.

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  1 in total

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Journal:  J Biol Chem       Date:  2009-04-06       Impact factor: 5.157

  1 in total

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