Fig. 1
- ID
- ZDB-FIG-240910-30
- Publication
- García-Cuesta et al., 2024 - Allosteric modulation of the CXCR4:CXCL12 axis by targeting receptor nanoclustering via the TMV-TMVI domain
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Screening for small compound antagonists acting at the oligomerization site of CXCR4. (A) Cartoon and surface representation of CXCR4 and the cleft identified between TMV and TMVI. The protein structure is shown in gray, with TMV and TMVI colored in blue and pink, respectively. In green, residues involved in CXCL12 binding. The cavity identified by SurfNet is shown in orange. Volume for the cavity is measured and shown in Å3. T4 lysozyme inserted between TMV and TMVI in the crystallized version of CXCR4 (PDB: 3ODU) is also shown in yellow. (B) Dose-response curve of the selected antagonists in Jurkat cell migration experiments in response to 12.5 nM CXCL12. Data are shown as percentage of migrating cells (mean ± SD; n=5; *≤0.05, *** p≤0.001, **** p≤0.0001). (C) Chemical structure of the selected compounds (AGR1.131, AGR1.135 and AGR1.137). The differences between the lateral chains of the three compounds are shaded in green. |