Structural highlights2yej is a 1 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: | 2cdd, 1yes, 1uy9, 1byq, 2bsm, 1osf, 2wi3, 1uy8, 2bug, 2wi4, 2uwd, 2xhx, 2wi7, 2bt0, 1yer, 2xdu, 1uyg, 2ccu, 2bz5, 2xds, 2xdx, 2ccs, 2xk2, 1yc3, 1uyi, 2xjj, 1uyf, 1uyd, 2byi, 2xdl, 2wi2, 2vci, 1uy6, 2wi1, 2vcj, 1yc4, 2xjx, 2fwz, 2xdk, 2c2l, 1uyk, 2xjg, 1uyh, 2cct, 2fwy, 1uye, 1uyl, 2xab, 2wi6, 1yc1, 1uy7, 2xhr, 1uyc, 2xht, 1yet, 2jjc, 2byh, 2wi5, 2ye2, 2ye3, 2ye4, 2ye5, 2ye6, 2ye7, 2ye8, 2ye9, 2yea, 2yeb, 2yec, 2yed, 2yee, 2yef, 2yeg, 2yeh, 2yei |
| 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]
See AlsoReferences
- ↑ 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
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