| Structural highlights
2bz5 is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | |
| Related: | 1byq, 1osf, 1uy6, 1uy7, 1uy8, 1uy9, 1uyc, 1uyd, 1uye, 1uyf, 1uyg, 1uyh, 1uyi, 1uyk, 1uyl, 1yc1, 1yc3, 1yc4, 1yer, 1yes, 1yet, 2bsm, 2bt0, 2byh, 2byi |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[HS90A_HUMAN] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Docking-based virtual screening identified 1-(2-phenol)-2-naphthol compounds as a new class of Hsp90 inhibitors of low to sub-micromolar potency. Here we report the binding affinities and cellular activities of several members of this class. A high resolution crystal structure of the most potent compound reveals its binding mode in the ATP binding site of Hsp90, providing a rationale for the observed activity of the series and suggesting strategies for developing compounds with improved properties.
Structure-based discovery of a new class of Hsp90 inhibitors.,Barril X, Brough P, Drysdale M, Hubbard RE, Massey A, Surgenor A, Wright L Bioorg Med Chem Lett. 2005 Dec 1;15(23):5187-91. Epub 2005 Oct 3. PMID:16202589[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Martinez-Ruiz A, Villanueva L, Gonzalez de Orduna C, Lopez-Ferrer D, Higueras MA, Tarin C, Rodriguez-Crespo I, Vazquez J, Lamas S. S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities. Proc Natl Acad Sci U S A. 2005 Jun 14;102(24):8525-30. Epub 2005 Jun 3. PMID:15937123 doi:10.1073/pnas.0407294102
- ↑ Forsythe HL, Jarvis JL, Turner JW, Elmore LW, Holt SE. Stable association of hsp90 and p23, but Not hsp70, with active human telomerase. J Biol Chem. 2001 May 11;276(19):15571-4. Epub 2001 Mar 23. PMID:11274138 doi:10.1074/jbc.C100055200
- ↑ Barril X, Brough P, Drysdale M, Hubbard RE, Massey A, Surgenor A, Wright L. Structure-based discovery of a new class of Hsp90 inhibitors. Bioorg Med Chem Lett. 2005 Dec 1;15(23):5187-91. Epub 2005 Oct 3. PMID:16202589 doi:10.1016/j.bmcl.2005.08.092
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