Protein folding in the central cavity of the GroEL-GroES chaperonin complex Journal Article
| Authors: | Mayhew, M.; da Silva, A. C. R.; Martin, J.; Erdjument-Bromage, H.; Tempst, P.; Hartl, F. U. |
| Article Title: | Protein folding in the central cavity of the GroEL-GroES chaperonin complex |
| Abstract: | The chaperonin GroEL is able to mediate protein folding in its central cavity. GroEL-bound dihydrofolate reductase assumes its native conformation when the GroES cofactor caps one end of the GroEL cylinder, thereby discharging the unfolded polypeptide into an enclosed cage. Folded dihydrofolate reductase emerges upon ATP-dependent GroES release. Other proteins, such as rhodanese, may leave GroEL after having attained a conformation that is committed to fold. Incompletely folded polypeptide rebinds to GroEL, resulting in structural rearrangement for another folding trial in the chaperonin cavity. |
| Keywords: | methotrexate; protein conformation; animals; mice; amino acid sequence; molecular sequence data; protein folding; protein structure; dihydrofolate reductase; tetrahydrofolate dehydrogenase; hydrolysis; models, chemical; cross linking; human; priority journal; article; chaperonin; groel protein; thiosulfate sulfurtransferase |
| Journal Title: | Nature |
| Volume: | 379 |
| Issue: | 6564 |
| ISSN: | 0028-0836 |
| Publisher: | Nature Publishing Group |
| Date Published: | 1996-02-01 |
| Start Page: | 420 |
| End Page: | 426 |
| Language: | English |
| PUBMED: | 8559246 |
| PROVIDER: | scopus |
| DOI: | 10.1038/379420a0 |
| DOI/URL: | |
| Notes: | Article -- Export Date: 22 November 2017 -- Source: Scopus |
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