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-Structure paper
Title | Design and SAR of macrocyclic Hsp90 inhibitors with increased metabolic stability and potent cell-proliferation activity. |
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Journal, issue, pages | Bioorg. Med. Chem. Lett., Vol. 21, Page 2278-2282, Year 2011 |
Publish date | Feb 22, 2011 (structure data deposition date) |
Authors | Zapf, C.W. / Bloom, J.D. / McBean, J.L. / Dushin, R.G. / Nittoli, T. / Ingalls, C. / Sutherland, A.G. / Sonye, J.P. / Eid, C.N. / Golas, J. ...Zapf, C.W. / Bloom, J.D. / McBean, J.L. / Dushin, R.G. / Nittoli, T. / Ingalls, C. / Sutherland, A.G. / Sonye, J.P. / Eid, C.N. / Golas, J. / Liu, H. / Boschelli, F. / Hu, Y. / Vogan, E. / Levin, J.I. |
External links | Bioorg. Med. Chem. Lett. / PubMed:21420297 |
Methods | X-ray diffraction |
Resolution | 1.5703 Å |
Structure data | PDB-3qtf: |
Chemicals | ChemComp-05S: ChemComp-DMS: ChemComp-HOH: |
Source |
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Keywords | CHAPERONE/CHAPERONE INHIBITOR / Chaperone / ATP binding domain / ATP-binding / Nucleotide-binding / Phosphoprotein / Stress response / CHAPERONE-CHAPERONE INHIBITOR complex |