The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site. Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Design and analysis of monomers and dimers. Dimerization of Hsp90 is required for in vivo function. Cryptic variation in morphological evolution: HSP90 as a capacitor for loss of eyes in cavefish. Hsp90 and environmental stress transform the adaptive value of natural genetic variation. Hsp90 as a capacitor of phenotypic variation. Shows that inhibition of the HSP90 orthologue Hsp83 in Drosophila results in a burst of phenotypic variation, which suggests that HSP90 controls the evolution of traits. Hsp90 as a capacitor for morphological evolution. HEAT SHOCK PROTEIN 90C is a bona fide Hsp90 that interacts with plastidic HSP70B in Chlamydomonas reinhardtii. The hsp90-related protein TRAP1 is a mitochondrial protein with distinct functional properties. Evolution and function of diverse Hsp90 homologs and cochaperone proteins. Comparative genomics and evolution of the HSP90 family of genes across all kingdoms of organisms. Regulation of human hsp90alpha gene expression. Essential role of the first intron in the transcription of hsp90βgene. ![]() Hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures. Identification of a transformation-specific antigen induced by an avian sarcoma virus. Steroid receptor interactions with heat shock protein and immunophilin chaperones. ![]() A number of these are currently being evaluated in clinical trials. The pleiotropic effects of HSP90 on diverse client proteins means that HSP90 is implicated in many diseases, most prominently cancer, neurodegenerative diseases and infectious diseases that are caused by viruses and protozoa.Ī number of HSP90 inhibitors have been identified that target the ATP-binding site or the carboxy-terminal domain. Within this broad range of clients, intrinsic instability and low folding cooperativity seem to dictate the requirement for the chaperone activity of HSP90. HSP90 clients are functionally and structurally diverse. Novel insights into client maturation have revealed that clients form contacts mainly with the middle domain of HSP90, but also make contacts with the amino-terminal and carboxy-terminal domains. HSP90 binds to clients in different conformations. Some co-chaperones introduce asymmetry in the symmetric HSP90 dimer. Co-chaperones modulate the rate of ATP hydrolysis by HSP90, stabilize certain conformational states or are involved in client recruitment. The highly dynamic conformational changes in the HSP90 dimer are regulated by a set of co-chaperones that bind to HSP90, often in different phases of its ATPase cycle. HSP90 clients include, among others, kinases, transcription factors, steroid hormone receptors and E3 ubiquitin ligases. ![]() Heat shock protein 90 (HSP90) is a molecular chaperone that is conserved from bacteria to humans and facilitates the maturation of substrates (or clients) that are involved in many different cellular pathways.
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