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Figure 3 - Structural insights into positive and negative allosteric regulation of a G protein-coupled receptor through protein-lipid interactions

Figure 3. Partial inactivation of the triad core of β2AR in a DOPC membrane. (A) RMSD profile of the conformational changes of the triad core: I 3.40 (red), P 5.50 (green) and F 6.44 (blue) over a 4 μs MD simulation in a DOPC membrane, compared to the active crystal structure (PDB id: 3SN6). (B) Superposition of the triad core observed at 4 μs compared to the active crystal structure triad core (orange, PDB id: 3SN6). Relevant residues are labelled: proline (P), isoleucine (I), phenylalanine (F) on transmembrane (TM) helices 3, 5, 6. 
Partial inactivation of the triad core of β2AR in a DOPC membrane. (A) RMSD profile of the conformational changes of the triad core: I 3.40 (red), P 5.50 (green) and F 6.44 (blue) over a 4 μs MD simulation in a DOPC membrane, compared to the active crystal structure (PDB id: 3SN6). (B) Superposition of the triad core observed at 4 μs compared to the active crystal structure triad core (orange, PDB id: 3SN6). Relevant residues are labelled: proline (P), isoleucine (I), phenylalanine (F) on transmembrane (TM) helices 3, 5, 6. 
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