Structure Determination of the N-Terminal Thioredoxin-like Domain of Protein Disulfide Isomerase Using Multidimensional Heteronuclear 13C/15N NMR Spectroscopy

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• 作者：Johan Kemmink ; Nigel J. Darby ; Klaas Dijkstra ; Michael Nilges ; and Thomas E. Creighton
• 刊名：Biochemistry
• 出版年：1996
• 出版时间：June 18, 1996
• 年：1996
• 卷：35
• 期：24
• 页码：7684 - 7691
• 全文大小：413K
• 年卷期：v.35,no.24(June 18, 1996)
• ISSN：1520-4995

文摘

As a first step in dissecting the structure of human proteindisulfide isomerase (PDI), thestructure of a fragment corresponding to the first 120 residues of itssequence has been determined usingheteronuclear multidimensional NMR techniques. As expected fromits primary structure homology, thefragment has the thioredoxin fold. Similarities and differences intheir structures help to explain whythioredoxins are reductants, whereas PDI is an oxidant of protein thiolgroups. The results confirm thatPDI has a modular, multidomain structure, which will facilitate itsstructural and functional characterization.