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' fragmen...

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Bibliographic Details
Published in:Biomolecular NMR assignments 2007-07, Vol.1 (1), p.129-130
Main Authors: Denisov, Alexey Yu, Maattanen, Pekka, Sprules, Tara, Thomas, David Y, Gehring, Kalle
Format: Article
Language:English
Subjects:
Binding Sites
Enzyme Stability
Enzymes
Humans
Molecular Structure
Nuclear Magnetic Resonance, Biomolecular
Peptide Fragments - chemistry
Peptide Fragments - genetics
Protein Disulfide-Isomerases - chemistry
Protein Disulfide-Isomerases - genetics
Protein Folding
Protein Structure, Tertiary
Recombinant Fusion Proteins - chemistry
Recombinant Fusion Proteins - genetics
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Summary: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.
ISSN:1874-2718
1874-270X
DOI:10.1007/s12104-007-9035-y