title: 1H, 13C and 15N resonance assignments of the bb' domains of human protein disulfide isomerase.
abstract: 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.
authors.affiliation: Department of Biochemistry, McGill University, Montreal, QC, Canada, H3G 1Y6.
authors.forename: Alexey Yu
authors.initials: AY
authors.lastname: Denisov
authors.forename: Pekka
authors.initials: P
authors.lastname: Maattanen
authors.forename: Tara
authors.initials: T
authors.lastname: Sprules
authors.forename: David Y
authors.initials: DY
authors.lastname: Thomas
authors.forename: Kalle
authors.initials: K
authors.lastname: Gehring
mesh_terms: 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
chemical_list: D010446:Peptide Fragments; D011993:Recombinant Fusion Proteins; D019704:Protein Disulfide-Isomerases