1H, 13C and 15N resonance assignments of the bb' domains of human protein disulfide isomerase.
Protein disulfide isomerase (PDI) participates in protein folding and catalyses formation of disulfide bonds. The b' domain of human PDI contributes to binding unfolded proteins; its structure is stabilized by the b domain. Here, we report NMR chemical shift assignments for the bb' fragment.
Denisov
Alexey Yu
AY
Department of Biochemistry, McGill University, Montreal, QC, Canada, H3G 1Y6.
Maattanen
Pekka
P
Sprules
Tara
T
Thomas
David Y
DY
Gehring
Kalle
K
D001665:Binding Sites; D004795:Enzyme Stability; D006801:Humans; D015394:Molecular Structure; D019906:Nuclear Magnetic Resonance, Biomolecular; D010446:Peptide Fragments / Q000737:chemistry / Q000235:genetics; D019704:Protein Disulfide-Isomerases / Q000737:chemistry* / Q000235:genetics; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics
D010446:Peptide Fragments; D011993:Recombinant Fusion Proteins; D019704:Protein Disulfide-Isomerases