| First Author | Buchner J | Year | 1999 |
| Journal | Trends Biochem Sci | Volume | 24 |
| Issue | 4 | Pages | 136-41 |
| PubMed ID | 10322418 | Mgi Jnum | J:54340 |
| Mgi Id | MGI:1334959 | Doi | 10.1016/s0968-0004(99)01373-0 |
| Citation | Buchner J (1999) Hsp90 & Co. - a holding for folding. Trends Biochem Sci 24(4):136-41 |
| abstractText | Hsp90 is an abundant molecular chaperone that is involved in the folding of a defined set of signalling molecules including steroid-hormone receptors and kinases. Recent in vitro experiments suggest that Hsp90 contains two different binding sites for non-native proteins, which allow it to combine the properties of a promiscuous chaperone with those of a dedicated folding-helper protein. Significant progress has been made in analysing co-chaperones, which form defined, substrate-dependent complexes with Hsp90 in vivo. Structural studies have identified the ATP-binding site in the N-terminal domain of Hsp90, which can be blocked by high-affinity inhibitors. Although a detailed understanding of the mechanism of Hsp90 action is still lacking, recent advances suggest that the protein is the centre of a dynamic, multifunctional and multicomponent chaperone machinery that extends the limits of protein folding in the cell. |
