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Structural biology. Crystal structure of the chemokine receptor CXCR4 in complex with a viral chemokine - PubMed
Source: pubmed.ncbi.nlm.nih.gov
Article summary:
1. The crystal structure of the chemokine receptor CXCR4 in complex with a viral chemokine, vMIP-II, has been determined at 3.1 angstrom resolution.
2. The structure revealed a 1:1 stoichiometry and a more extensive binding interface than anticipated from the paradigmatic two-site model.
3. The structure helped rationalize a large body of mutagenesis data and provided insights into CXCR4 interactions with its endogenous ligand CXCL12, its ability to recognize diverse ligands, and the specificity of CC and CXC receptors for their respective chemokines.
Article analysis:
The article is generally reliable and trustworthy as it is published in Science, one of the most prestigious scientific journals in the world. It is also written by an experienced team of researchers from various institutions who have conducted extensive research on this topic. Furthermore, the article provides detailed information about the methods used to determine the crystal structure of CXCR4 in complex with vMIP-II as well as results from experiments that support their findings.
However, there are some potential biases that should be noted when reading this article. For example, it does not provide any information about possible risks associated with using this receptor or any counterarguments to their findings. Additionally, it does not present both sides equally; instead it focuses mainly on supporting evidence for their claims without exploring other possibilities or alternative explanations for their results. Finally, there may be some promotional content in the article as it highlights the importance of understanding how chemokines interact with their receptors which could lead to new treatments for diseases such as inflammation and cancer.