人蛋白质二硫键异构酶bb'结构域的1H、13C和15N共振归属

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

作者信息

Denisov Alexey Yu, Maattanen Pekka, Sprules Tara, Thomas David Y, Gehring Kalle

机构信息

Department of Biochemistry, McGill University, Montreal, QC, Canada, H3G 1Y6.

出版信息

Biomol NMR Assign. 2007 Jul;1(1):129-30. doi: 10.1007/s12104-007-9035-y. Epub 2007 Aug 7.

DOI:10.1007/s12104-007-9035-y

PMID:19636846

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.

摘要

蛋白质二硫键异构酶（PDI）参与蛋白质折叠并催化二硫键的形成。人PDI的b'结构域有助于结合未折叠的蛋白质；其结构由b结构域稳定。在此，我们报告了bb'片段的核磁共振化学位移归属。