3Q6M

Crystal Structure of Human MC-HSP90 in C2221 Space Group

Summary for 3Q6M

Entry DOI	10.2210/pdb3q6m/pdb
Related	3Q6N
Descriptor	Heat shock protein HSP 90-alpha, SULFATE ION (3 entities in total)
Functional Keywords	three domains, trimer of dimer, hexamer, chaperone
Biological source	Homo sapiens (human)
Cellular location	Cytoplasm: P07900
Total number of polymer chains	3
Total formula weight	157402.83
Authors	Lee, C.C.,Lin, T.W.,Ko, T.P.,Wang, A.H.-J. (deposition date: 2011-01-03, release date: 2011-06-01, Last modification date: 2023-11-01)
Primary citation	Lee, C.C.,Lin, T.W.,Ko, T.P.,Wang, A.H.-J. The hexameric structures of human heat shock protein 90 Plos One, 6:e19961-e19961, 2011 Cited by PubMed Abstract: The human 90-kDa heat shock protein (HSP90) functions as a dimeric molecular chaperone. HSP90 identified on the cell surface has been found to play a crucial role in cancer invasion and metastasis, and has become a validated anti-cancer target for drug development. It has been shown to self-assemble into oligomers upon heat shock or divalent cations treatment, but the functional role of the oligomeric states in the chaperone cycle is not fully understood. PubMed: 21647436 DOI: 10.1371/journal.pone.0019961 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (3 Å)

Structure validation