1US7: Complex Of Hsp90 And P50

Recruitment of protein kinase clients to the Hsp90 chaperone involves the cochaperone p50(cdc37) acting as a scaffold, binding protein kinases via its N-terminal domain and Hsp90 via its C-terminal region. p50(cdc37) also has a regulatory activity, arresting Hsp90's ATPase cycle during client-protein loading. We have localized the binding site for p50(cdc37) to the N-terminal nucleotide binding domain of Hsp90 and determined the crystal structure of the Hsp90-p50(cdc37) core complex. Dimeric p50(cdc37) binds to surfaces of the Hsp90 N-domain implicated in ATP-dependent N-terminal dimerization and association with the middle segment of the chaperone. This interaction fixes the lid segment in an open conformation, inserts an arginine side chain into the ATP binding pocket to disable catalysis, and prevents trans-activating interaction of the N domains.
PDB ID: 1US7Download
MMDB ID: 26274
PDB Deposition Date: 2003/11/20
Updated in MMDB: 2012/10
Experimental Method:
x-ray diffraction
Resolution: 2.3  Å
Source Organism:
Homo sapiens
Similar Structures:
Biological Unit for 1US7: dimeric; determined by author and by software (PQS)
Molecular Components in 1US7
Label Count Molecule
Proteins (2 molecules)
Heat Shock Protein Hsp82(Gene symbol: HSP82)
Molecule annotation
Hsp90 Co-chaperone Cdc37(Gene symbol: CDC37)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB