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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...
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| Main Authors: | , , , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado: |
American Society for Biochemistry and Molecular Biology
2008
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| Assuntos: | |
| Acceso en liña: | 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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