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The article provides a detailed description of a novel evolutionarily conserved domain of cell-adhesion GPCRs, called the GPCR-Autoproteolysis INducing (GAIN) domain. The authors provide evidence for their claims through crystal structures of GAIN domains from two distantly related cell-adhesion GPCRs, which revealed a conserved novel fold in which the GPS motif forms five β-strands that are tightly integrated into the overall GAIN domain. Furthermore, they demonstrate that this GAIN domain is both necessary and sufficient for autoproteolysis, suggesting an autoproteolytic mechanism whereby the overall GAIN domain fine-tunes the chemical environment in the GPS to catalyse peptide bond hydrolysis.

The article appears to be well researched and reliable as it provides evidence for its claims through crystal structures and functional experiments. Furthermore, it cites relevant literature throughout its discussion section to support its claims. However, there are some potential biases that should be noted when evaluating this article's trustworthiness and reliability. For example, while it does cite relevant literature throughout its discussion section, it does not explore any counterarguments or present any opposing views on its claims or conclusions. Additionally, while it does mention potential risks associated with its findings (e.g., multiple human disease mutations), it does not provide any further detail or exploration into these risks or their implications. Finally, while it does provide evidence for its claims through crystal structures and functional experiments, it does not provide any further detail or exploration into how these experiments were conducted or what results were obtained from them.