1H, 13C and 15N resonance assignments of the bb′ domains of human protein disulfide isomerase

被引：0
|
作者：
Alexey Yu. Denisov
Pekka Maattanen
Tara Sprules
David Y. Thomas
Kalle Gehring
机构：
[1] McGill University,Department of Biochemistry
[2] McGill University,Quebec/Eastern Canada High Field NMR Facility
来源：
Biomolecular NMR Assignments | 2007年 / 1卷
关键词：
Endoplasmic reticulum; Protein folding; Disulfide bonds; PDI;
D O I：
暂无
中图分类号：
学科分类号：
摘要：
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.
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页码：129 / 130
页数：1
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