Effects of the COVID-19 pandemic on SCUBA diving experience in marine protected areas.

Faced with the need for isolation of most people to reduce the transmission of COVID-19, a great concern for the well-being of the population has resurfaced. Considering the numerous benefits of outdoor activities to human health and well-being, we assessed whether the quality of the experience of recreational divers in a marine protected area (MPA) was impacted during the pandemic. We applied a semi-structured questionnaire to divers, collected their socioeconomic profile, preferences, motivations, experiences, and compared the results with those obtained in the previous season. We found that the quality of the recreational diver's experience remained high even during one of the world's biggest health crises. This suggests that the combination of contact with a preserved environment and the adaptation of regulations in favor of visitor safety was enough to stimulate positive experiences. Therefore, we highlight the importance of investing in adaptive management so that MPAs continue to promote ecosystem services such as human health and subjective well-being. Management implications: •Quality of experience for recreational divers remained high and was unaffected after the first major wave of COVID-19 cases.•Through adaptive tourism management, MPAs can promote positive experiences even in challenging contexts.•High impact of environmental attributes on the quality of divers' experience reinforces that threats to ecosystems are social impacts.•Socially unequal access to benefits generated by MPAs may negatively influence population's support for these areas.•Efforts are needed to strengthen the equity of distribution of positive social impacts in MPAs.•Potential to provide positive experiences for users must be seen beyond economic value, but as an investment in the population's subjective well-being.

Crystal structure of the tyrosine kinase domain of the hepatocyte growth factor receptor c-Met and its complex with the microbial alkaloid K-252a.

The protooncogene c-met codes for the hepatocyte growth factor receptor tyrosine kinase. Binding of its ligand, hepatocyte growth factor/scatter factor, stimulates receptor autophosphorylation, which leads to pleiotropic downstream signaling events in epithelial cells, including cell growth, motility, and invasion. These events are mediated by interaction of cytoplasmic effectors, generally through Src homology 2 (SH2) domains, with two phosphotyrosine-containing sequence motifs in the unique C-terminal tail of c-Met (supersite). There is a strong link between aberrant c-Met activity and oncogenesis, which makes this kinase an important cancer drug target. The furanosylated indolocarbazole K-252a belongs to a family of microbial alkaloids that also includes staurosporine. It was recently shown to be a potent inhibitor of c-Met. Here we report the crystal structures of an unphosphorylated c-Met kinase domain harboring a human cancer mutation and its complex with K-252a at 1.8-A resolution. The structure follows the well established architecture of protein kinases. It adopts a unique, inhibitory conformation of the activation loop, a catalytically noncompetent orientation of helix alphaC, and reveals the complete C-terminal docking site. The first SH2-binding motif (1349YVHV) adopts an extended conformation, whereas the second motif (1356YVNV), a binding site for Grb2-SH2, folds as a type II Beta-turn. The intermediate portion of the supersite (1353NATY) assumes a type I Beta-turn conformation as in an Shc-phosphotyrosine binding domain peptide complex. K-252a is bound in the adenosine pocket with an analogous binding mode to those observed in previously reported structures of protein kinases in complex with staurosporine.