The crystal structure of the protein-disulfide isomerase family member ERp27 provides insights into its substrate binding capabilities

Journal of Biological Chemistry

Volumn 288, Issue 3, 2013, Pages 2029-2039

  Xaver Kober, Franz ^a   Koelmel, Wolfgang ^a   Kuper, Jochen ^a   Drechsler, Johannes ^a   Mais, Christine ^a   Hermanns, Heike M ^a   Schindelin, Hermann ^a  

^a UNIVERSITY OF WÜRZBURG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CELLULAR PROTEINS; CONFORMATIONAL CHANGE; DISULFIDE BONDS; ENDOPLASMIC RETICULUM; ER STRESS; ISOTHERMAL TITRATION CALORIMETRY; MISFOLDED PROTEINS; OXIDATIVE FOLDING; PROTEIN DISULFIDE ISOMERASES; SECRETORY PATHWAYS; STRESS CONDITION; SUBSTRATE-BINDING; SUBSTRATE-BINDING SITES;

AMINO ACIDS; CELL MEMBRANES; COVALENT BONDS; PROTEIN FOLDING; PROTEINS;

SUBSTRATES;

CELL PROTEIN; CYSTEINE; DISULFIDE; ISOMERASE;

ARTICLE; BINDING SITE; CATALYSIS; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; DISULFIDE BOND; ENDOPLASMIC RETICULUM STRESS; ENZYME SUBSTRATE COMPLEX; HYDROPHOBICITY; ISOMERIZATION; ISOTHERMAL TITRATION CALORIMETRY; OXIDATION REDUCTION STATE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; PROTEIN STRUCTURE;

BINDING SITES; BIOCATALYSIS; CALORIMETRY; CELL LINE, TUMOR; CRYSTALLOGRAPHY, X-RAY; DISULFIDES; ENDOPLASMIC RETICULUM; ENDOPLASMIC RETICULUM STRESS; HUMANS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MODELS, MOLECULAR; MOLECULAR CHAPERONES; OXIDATION-REDUCTION; PROTEIN BINDING; PROTEIN DISULFIDE-ISOMERASES; PROTEIN FOLDING; PROTEINS;

EID: 84872744555     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.410522     Document Type: Article

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