1uyl
From Proteopedia
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| - | [[Image:1uyl.jpg|left|200px]] | + | [[Image:1uyl.jpg|left|200px]] |
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| - | '''STRUCTURE-ACTIVITY RELATIONSHIPS IN PURINE-BASED INHIBITOR BINDING TO HSP90 ISOFORMS''' | + | {{Structure |
| + | |PDB= 1uyl |SIZE=350|CAPTION= <scene name='initialview01'>1uyl</scene>, resolution 1.40Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''STRUCTURE-ACTIVITY RELATIONSHIPS IN PURINE-BASED INHIBITOR BINDING TO HSP90 ISOFORMS''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1UYL is a [ | + | 1UYL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UYL OCA]. |
==Reference== | ==Reference== | ||
| - | Structure-activity relationships in purine-based inhibitor binding to HSP90 isoforms., Wright L, Barril X, Dymock B, Sheridan L, Surgenor A, Beswick M, Drysdale M, Collier A, Massey A, Davies N, Fink A, Fromont C, Aherne W, Boxall K, Sharp S, Workman P, Hubbard RE, Chem Biol. 2004 Jun;11(6):775-85. PMID:[http:// | + | Structure-activity relationships in purine-based inhibitor binding to HSP90 isoforms., Wright L, Barril X, Dymock B, Sheridan L, Surgenor A, Beswick M, Drysdale M, Collier A, Massey A, Davies N, Fink A, Fromont C, Aherne W, Boxall K, Sharp S, Workman P, Hubbard RE, Chem Biol. 2004 Jun;11(6):775-85. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15217611 15217611] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: hsp90]] | [[Category: hsp90]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:38:38 2008'' |
Revision as of 12:38, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE-ACTIVITY RELATIONSHIPS IN PURINE-BASED INHIBITOR BINDING TO HSP90 ISOFORMS
Overview
Inhibition of the ATPase activity of the chaperone protein HSP90 is a potential strategy for treatment of cancers. We have determined structures of the HSP90alpha N-terminal domain complexed with the purine-based inhibitor, PU3, and analogs with enhanced potency both in enzyme and cell-based assays. The compounds induce upregulation of HSP70 and downregulation of the known HSP90 client proteins Raf-1, CDK4, and ErbB2, confirming that the molecules inhibit cell growth by a mechanism dependent on HSP90 inhibition. We have also determined the first structure of the N-terminal domain of HSP90beta, complexed with PU3. The structures allow a detailed rationale to be developed for the observed affinity of the PU3 class of compounds for HSP90 and also provide a structural framework for design of compounds with improved binding affinity and drug-like properties.
About this Structure
1UYL is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure-activity relationships in purine-based inhibitor binding to HSP90 isoforms., Wright L, Barril X, Dymock B, Sheridan L, Surgenor A, Beswick M, Drysdale M, Collier A, Massey A, Davies N, Fink A, Fromont C, Aherne W, Boxall K, Sharp S, Workman P, Hubbard RE, Chem Biol. 2004 Jun;11(6):775-85. PMID:15217611
Page seeded by OCA on Thu Mar 20 14:38:38 2008
Categories: Homo sapiens | Single protein | Aherne, W. | Barril, X. | Beswick, M. | Boxall, K. | Collier, A. | Davies, N. | Drysdale, M. | Dymock, B. | Fink, A. | Fromont, C. | Hubbard, R E. | Massey, A. | Sharp, S. | Sheridan, L. | Surgenor, A. | Workman, P. | Wright, L. | Atp-binding | Atpase | Chaperone | Heat shock | Hsp90
