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Structural biology. Structural basis for chemokine recognition and activation of a viral G protein-coupled receptor - PubMed
Source: pubmed.ncbi.nlm.nih.gov
Article summary:
1. The crystal structure of the human cytomegalovirus GPCR US28 in complex with the chemokine domain of human CX3CL1 (fractalkine) has been determined at 2.9 angstrom resolution.
2. The globular body of CX3CL1 is perched on top of the US28 extracellular vestibule, whereas its amino terminus projects into the central core of US28.
3. Atomic-level simulations suggest that the agonist-independent activity of US28 may be due to an amino acid network evolved in the viral GPCR to destabilize the receptor's inactive state.
Article analysis:
The article is a scientific paper published in Science magazine and is thus considered reliable and trustworthy. The authors have provided evidence for their claims through detailed descriptions and figures, as well as atomic-level simulations which support their conclusions. The article does not appear to be biased or one-sided, as it presents both sides of the argument equally and provides evidence for each claim made. Furthermore, there are no unsupported claims or missing points of consideration, as all relevant information is included in the paper. Additionally, there is no promotional content or partiality present in the article, and possible risks are noted throughout. Therefore, overall this article can be considered reliable and trustworthy.