The human protein disulphide isomerase family: substrate interactions and functional properties

被引：668

作者：

Ellgaard, L

Ruddock, LW

机构：

[1] Univ Oulu, Dept Biochem, Oulu 90014, Finland

[2] Swiss Fed Inst Technol, Inst Biochem, CH-8093 Zurich, Switzerland

[3] Univ Oulu, Bioctr Oulu, Oulu 90014, Finland

来源：

EMBO REPORTS | 2005年 / 6卷 / 01期

关键词：

D O I：

10.1038/sj.embor.7400311

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

The process of disulphide bond formation in the endoplasmic reticulum of eukaryotic cells was one of the first mechanisms of catalysed protein folding to be discovered. Protein disulphide isomerase (PDI) is now known to catalyse all of the reactions that are involved in native disulphide bond formation, but despite more than 40 years of study, its mechanism of action is still not fully understood. This review discusses recent advances in our understanding of the human PDI family of enzymes and focuses on their functional properties, substrate interactions and some recently identified family members.

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页码：28 / 32

页数：5

相关论文

共 36 条

[1]

Functional characterization of ERp18, a new endoplasmic reticulum-located thioredoxin superfamily member [J].

Alanen, HI ;

Williamson, RA ;

Howard, MJ ;

Lappi, AK ;

Jäntti, HP ;

Rautio, SM ;

Kellokumpu, S ;

Ruddock, LW .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (31) :28912-28920

[2]

ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family [J].

Anelli, T ;

Alessio, M ;

Mezghrani, A ;

Simmen, T ;

Talamo, F ;

Bachi, A ;

Sitia, R .

EMBO JOURNAL, 2002, 21 (04) :835-844

[3]

Thiol-mediated protein retention in the endoplasmic reticulum: the role of ERp44 [J].

Anelli, T ;

Alessio, M ;

Bachi, A ;

Bergamelli, L ;

Bertoli, G ;

Camerini, S ;

Mezghrani, A ;

Ruffato, E ;

Simmen, T ;

Sitia, R .

EMBO JOURNAL, 2003, 22 (19) :5015-5022

[4]

Mapping of a substrate binding site in the protein disulfide isomerase-related chaperone wind based on protein function and crystal structure [J].

Barnewitz, K ;

Guo, CS ;

Sevvana, M ;

Ma, GJ ;

Sheldrick, GM ;

Söling, HD ;

Ferrari, DM .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (38) :39829-39837

[5]

ERdJ5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stress [J].

Cunnea, PM ;

Miranda-Vizuete, A ;

Bertoli, G ;

Simmen, T ;

Damdimopoulos, AE ;

Hermann, S ;

Leinonen, S ;

Huikko, MP ;

Gustafsson, JÅ ;

Sitia, R ;

Spyrou, G .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (02) :1059-1066

[6]

The multi-domain structure of protein disulfide isomerase is essential for high catalytic efficiency [J].

Darby, NJ ;

Penka, E ;

Vincentelli, R .

JOURNAL OF MOLECULAR BIOLOGY, 1998, 276 (01) :239-247

[7]

Effects of buried charged groups on cysteine thiol ionization and reactivity in Escherichia coli thioredoxin: Structural and functional characterization of mutants of Asp 26 and Lys 57 [J].

Dyson, HJ ;

Jeng, MF ;

Tennant, LL ;

Slaby, I ;

Lindell, M ;

Cui, DS ;

Kuprin, S ;

Holmgren, A .

BIOCHEMISTRY, 1997, 36 (09) :2622-2636

[8]

NMR structure of the calreticulin P-domain [J].

Ellgaard, L ;

Riek, R ;

Herrmann, T ;

Güntert, P ;

Braun, D ;

Helenius, A ;

Wüthrich, K .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (06) :3133-3138

[9]

The protein disulphide-isomerase family:: unravelling a string of folds [J].

Ferrari, DM ;

Söling, HD .

BIOCHEMICAL JOURNAL, 1999, 339 :1-10

[10]

Protein disulfide isomerases exploit synergy between catalytic and specific binding domains [J].

Freedman, RB ;

Klappa, P ;

Ruddock, LW .

EMBO REPORTS, 2002, 3 (02) :136-140

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