The prehensile-tailed skink Corucia zebrata is endemic to the Solomon Islands. It is the most traded reptile from the country. During 2000–2019, CITES reported the legal export of 10,567 individuals. Although the level of this trade is well documented, impacts on the skink's survival in its native range are comparatively unknown. During January–May 2020, we surveyed 146 people on 12 islands to collect information on the habitats preferred by the prehensile-tailed skink, to understand perceptions of the species' conservation status and identify any potential threats. Respondents reported lowland and hill forests as being favoured habitats, with low proportions of respondents identifying coastal and montane forests as suitable habitat. Habitat loss (72%), hunting (17%), and predation (6%) were identified as the main threats. People younger than 30 years of age reported killing the skinks more frequently than did people over the age of 30. Prehensile-tailed skinks have a relatively small home range, long reproductive cycle, and are vulnerable to numerous threats. We thus recommend a halt to the current practice of exporting wild-caught prehensile-tailed skinks, and replacement by a well-regulated captive breeding programme.

The ubiquitous molecular chaperone Hsp90 makes up 1–2% of cytosolic proteins and is required for viability in eukaryotes. Hsp90 affects the folding and activation of a wide variety of substrate proteins including many involved in signaling and regulatory processes. Some of these substrates are implicated in cancer and other diseases, making Hsp90 an attractive drug target. Structural analyses have shown that Hsp90 is a highly dynamic and flexible molecule that can adopt a wide variety of structurally distinct states. One driving force for these rearrangements is the intrinsic ATPase activity of Hsp90, as seen with other chaperones. However, unlike other chaperones, studies have shown that the ATPase cycle of Hsp90 is not conformationally deterministic. That is, rather than dictating the conformational state, ATP binding and hydrolysis only shift the equilibria between a pre-existing set of conformational states. For bacterial, yeast and human Hsp90, there is a conserved three-state (apo–ATP–ADP) conformational cycle; however; the equilibria between states are species specific. In eukaryotes, cytosolic co-chaperones regulate the in vivo dynamic behavior of Hsp90 by shifting conformational equilibria and affecting the kinetics of structural changes and ATP hydrolysis. In this review, we discuss the structural and biochemical studies leading to our current understanding of the conformational dynamics of Hsp90, as well as the roles that nucleotide, co-chaperones, post-translational modification and substrates play. This view of Hsp90's conformational dynamics was enabled by the use of multiple complementary structural methods including, crystallography, small-angle X-ray scattering (SAXS), electron microscopy, Förster resonance energy transfer (FRET) and NMR. Finally, we discuss the effects of Hsp90 inhibitors on conformation and the potential for developing small molecules that inhibit Hsp90 by disrupting the conformational dynamics.