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- W2088398459 abstract "Significance The chemokine receptor axis plays a critical role in numerous physiological and pathological processes, yet the structural basis of receptor interaction with chemokines is poorly understood. Although the community agrees on the existence of two distinct epitopes for recognition of receptors by chemokines, conflicting evidence from structural and mutagenesis studies suggested several possibilities for receptor:chemokine complex stoichiometry. We use a combination of computational, functional, and biophysical approaches to show that despite its dimeric nature, chemokine receptor CXCR4 interacts with its chemokine ligand, CXCL12, in a 1:1 stoichiometry. This result is also likely relevant for other receptor:chemokine pairs. Structural modeling informed by restraints derived from cysteine trapping experiments enabled determination of the receptor:chemokine complex geometry at a medium resolution level." @default.
- W2088398459 created "2016-06-24" @default.
- W2088398459 creator A5004550798 @default.
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- W2088398459 date "2014-12-02" @default.
- W2088398459 modified "2023-10-16" @default.
- W2088398459 title "Stoichiometry and geometry of the CXC chemokine receptor 4 complex with CXC ligand 12: Molecular modeling and experimental validation" @default.
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- W2088398459 doi "https://doi.org/10.1073/pnas.1417037111" @default.
- W2088398459 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4273337" @default.
- W2088398459 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25468967" @default.
- W2088398459 hasPublicationYear "2014" @default.