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Figure 1

Figure 1. From: Building a new conceptual framework for receptor heteromers.

Examples of heteromeric receptors, receptor heteromers and receptors with associated modifying proteins. (a) The glutamate NMDA receptor as an example of a heteromeric ionotropic receptor. The NMDA receptor is a tetrameric complex formed by NR1 and NR2 subunits (only two subunits are shown) that bind glycine and glutamate, respectively8. (b) The GABAB receptor heteromeric receptor as an example of a heteromeric GPCR. GABAB1 and GABAB2 subunits establish coiled-coil interactions between their C termini2. (c) The A2A-D2 receptor heteromer. The C terminus of the adenosine A2A receptor binds to the long third intracellular loop of the dopamine D2 receptor3; whether this and other receptor heteromers are dimeric or higher order oligomeric species remains to be established. (d) The D1-NMDA receptor heteromer, as an example of a receptor heteromer with a heteromeric receptor as one of the receptor units; the C termini of the NR1 and NR2 (NR2A) subunits bind to different epitopes of the C terminus of the dopamine D1 receptor14. (e) The MT1-GPR50 receptor, formed by the association of the melatonin MT1 receptor and the orphan 7TM protein GPR50. TM domains are probably involved in the oligomerization, while the long C terminus of GPR50 is mostly involved in the modulation of MT1 receptor function15. (f) The amylin (AMY) receptor, formed by the oligomerization of the calcitonin (CT) receptor and the single transmembrane protein RAMP; the two proteins bind through their N-terminal domains16. In bf, two subunits are shown for schematic purposes, without ruling out multimerization.

Sergi Ferré, et al. Nat Chem Biol. ;5(3):131-134.

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