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  The Human Cdc37·Hsp90 Complex Studied by Heteronuclear NMR Spectroscopy

Sreeramulu, S., Jonker, H. R. A., Langer, T., Richter, C., Lancaster, C. R. D., & Schwalbe, H. (2009). The Human Cdc37·Hsp90 Complex Studied by Heteronuclear NMR Spectroscopy. The Journal of Biological Chemistry, 284(6), 3885-3896.

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Datensatz-Permalink: https://hdl.handle.net/11858/00-001M-0000-0024-D779-8 Versions-Permalink: https://hdl.handle.net/11858/00-001M-0000-0024-D77A-6
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 Urheber:
Sreeramulu, Sridhar, Autor
Jonker, Hendrik R. A., Autor
Langer, Thomas, Autor
Richter, Christian, Autor
Lancaster, C. Roy D.1, Autor           
Schwalbe, Harald, Autor
Affiliations:
1Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              

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 Zusammenfassung: The cell division cycle protein 37 (Cdc37) and the 90-kDa heat shock protein (Hsp90) are molecular chaperones, which are crucial elements in the protein signaling pathway. The largest class of client proteins for Cdc37 and Hsp90 are protein kinases. The catalytic domains of these kinases are stabilized by Cdc37, and their proper folding and functioning is dependent on Hsp90. Here, we present the x-ray crystal structure of the 16-kDa middle domain of human Cdc37 at 1.88A˚ resolution and the structure of this domain in complex with the 23-kDa N-terminal domain of human Hsp90 based on heteronuclear solution state NMR data and docking. Our results demonstrate that the middle domain of Cdc37 exists as a monomer. NMR and mutagenesis experiments reveal Leu-205 in Cdc37 as a key residue enabling complex formation. These findings can be very useful in the development of small molecule inhibitors against cancer

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Sprache(n): eng - English
 Datum: 2009-02-06
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: eDoc: 473579
 Art des Abschluß: -

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Titel: The Journal of Biological Chemistry
  Alternativer Titel : J. Biol. Chem.
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 284 (6) Artikelnummer: - Start- / Endseite: 3885 - 3896 Identifikator: -