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

被引：4

作者：

Denisov, Alexey Yu. ^{[1
]}

Maattanen, Pekka ^{[1
]}

Sprules, Tara ^{[2
]}

Thomas, David Y. ^{[1
]}

Gehring, Kalle ^{[1
,2
]}

机构：

[1] McGill Univ, Dept Biochem, Montreal, PQ H3G 1Y6, Canada

[2] McGill Univ, Quebec Eastern Canada High Field NMR Facil, Montreal, PQ H3G 1Y6, Canada

来源：

BIOMOLECULAR NMR ASSIGNMENTS | 2007年 / 1卷 / 01期

基金：

加拿大健康研究院;

关键词：

endoplasmic reticulum; protein folding; disulfide bonds; PDI;

D O I：

10.1007/s12104-007-9035-y

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 [生物物理学];

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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收藏

页码：129 / 130

页数：2

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