The Catalytic Activity of Protein-disulfide Isomerase Requires a Conformationally Flexible Molecule

Protein-disulfide isomerase (PDI) catalyzes the formation of the correct pattern of disulfide bonds in secretory proteins. A low resolution crystal structure of yeast PDI described here reveals large scale conformational changes compared with the initially reported structure, indicating that PDI is...

Deskribapen osoa

Gorde:
Xehetasun bibliografikoak
Egile Nagusiak: Tian, Geng, Kober, Franz-Xaver, Lewandrowski, Urs, Sickmann, Albert, Lennarz, William J., Schindelin, Hermann
Formatua: Artigo
Hizkuntza:Inglês
Argitaratua: American Society for Biochemistry and Molecular Biology 2008
Gaiak:
Protein Synthesis, Post-Translational Modification, and Degradation
Sarrera elektronikoa:https://ncbi.nlm.nih.gov/pmc/articles/PMC2586259/
https://ncbi.nlm.nih.gov/pubmed/18815132
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M806026200
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