Fig. 3: Cholesterol molecules in CXCR4 homodimeric structure B. | Nature Communications

Fig. 3: Cholesterol molecules in CXCR4 homodimeric structure B.

From: Structural basis of dimerization of chemokine receptors CCR5 and CXCR4

Fig. 3

A High-density regions of cholesterol molecules around the CXCR4 monomers are represented as 2D extracellular view (Top Left) and 3D atomistic structure (Bottom Left). B Additional high-density regions are present in both protomers, not at the dimer interface; some of those are also found in the monomeric state. C Atomistic detail of the cholesterol molecule stabilizing the CXCR4 dimeric structure B represented as gray sticks together with its interacting residues. The dimeric structure B of CXCR4 hosts a binding site for cholesterol shaped by TM3-TM5 for one protomer and TM5-TM6 for the other, where polar and hydrophobic interactions are formed. Further discussion on the role of cholesterol in CXCR4 and CCR5 monomeric and dimeric forms is reported in the Supplementary Information. The color code of TM helices is the same reported in Fig. 1.

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