Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy.
As a first step in dissecting the structure of human protein disulfide isomerase (PDI), the structure of a fragment corresponding to the first 120 residues of its sequence has been determined using heteronuclear multidimensional NMR techniques. As expected from its primary structure homology, the fragment has the thioredoxin fold. Similarities and differences in their structures help to explain why thioredoxins are reductants, whereas PDI is an oxidant of protein thiol groups. The results confirm that PDI has a modular, multidomain structure, which will facilitate its structural and functional characterization.
Kemmink
J
J
European Molecular Biology Laboratory, Heidelberg, Germany.
Darby
N J
NJ
Dijkstra
K
K
Nilges
M
M
Creighton
T E
TE
D000595:Amino Acid Sequence; D002247:Carbon Isotopes; D003001:Cloning, Molecular; D003198:Computer Simulation; D004926:Escherichia coli / Q000378:metabolism; D006801:Humans; D007535:Isomerases / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008961:Models, Structural; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes; D011487:Protein Conformation; D019704:Protein Disulfide-Isomerases; D011994:Recombinant Proteins / Q000737:chemistry; D017386:Sequence Homology, Amino Acid; D012984:Software; D013879:Thioredoxins / Q000737:chemistry*
D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D011994:Recombinant Proteins; D013879:Thioredoxins; D007535:Isomerases; D019704:Protein Disulfide-Isomerases