Heat shock protein HSP 90-alpha (HSP90AA1) is a ~84 kDa protein. 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 which is essential for its chaperone 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. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. 1. Forsythe, HL. et al. (2001) The Journal of biological chemistry 276, 15571-4. PMID: 112741384. Martínez-Ruiz, A. et al. (2005) Proceedings of the National Academy of Sciences of the United States of America 102, 8525-30. PMID: 159371235. Woodford, MR. et al. (2016) Nature communications 7, 12037. PMID: 273533606. Woodford, MR. et al. (2017) The EMBO journal 36, 3650-3665. PMID: 291271559. Khurana, N. et al. (2015) Frontiers in oncology 5, 100. PMID: 2597339710. Triantafilou, K. et al. (2001) Nature immunology 2, 338-45. PMID: 11276205 | 
