2W0G

HSP90 CO-CHAPERONE CDC37

Summary for 2W0G

• Entry DOI: 10.2210/pdb2w0g/pdb
• Related: 1US7
• Descriptor: HSP90 CO-CHAPERONE CDC37 (2 entities in total)
• Functional Keywords: chaperone, heat shock, atp-binding, stress response, nucleotide-binding, phosphoprotein, phosphorylation, chaperone co-chaperone regulation
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cytoplasm : Q16543
• Total number of polymer chains: 1
• Total formula weight: 15521.08

Authors

Sreeramulu, S.,Jonker, H.R.A.,Schwalbe, H.,Lancaster, C.R.D. (deposition date: 2008-08-15, release date: 2008-12-09, Last modification date: 2023-12-13)

Primary citation

Sreeramulu, S.,Jonker, H.R.A.,Richter, C.,Langer, T.,Lancaster, C.R.D.,Schwalbe, H.
The Human Cdc37.Hsp90 Complex Studied by Heteronuclear NMR Spectroscopy.
J.Biol.Chem., 284:3885-, 2009

PubMed Abstract: 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 1.88 angstroms 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.

PubMed: 19073599
DOI: 10.1074/JBC.M806715200

Experimental method

X-RAY DIFFRACTION (1.88 Å)