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- W2116714781 abstract "Chemokine receptors are heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptors (GPCR) that play fundamental roles in many physiological and pathological processes. Typically, these receptors form a seven-transmembrane helix bundle, which is stabilized by a disulfide bond bridging the top of the third transmembrane segment (TM3) and the second extracellular loop (ECL2). Resolution of the three-dimensional structures of the chemokine receptors CXCR1, CXCR4, and CCR5 revealed the existence of a second disulfide bridge that links the N terminus of the receptor to the top of the seventh transmembrane segment (TM7), thereby closing the receptor into a ring. An important consequence of this second disulfide bond is the formation of an additional extracellular loop, which shapes the entrance of the ligand-binding pocket and adds rigidity to the overall surface of the receptor. Here, we discuss the features of these pseudo-loops, the structural requirements for their formation, and the effects they may have on receptor function." @default.
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- W2116714781 date "2014-09-02" @default.
- W2116714781 modified "2023-10-14" @default.
- W2116714781 title "Closing the Ring: A Fourth Extracellular Loop in Chemokine Receptors" @default.
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- W2116714781 doi "https://doi.org/10.1126/scisignal.2005664" @default.
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