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& Hoffman, H
GLP-1R interactions with G s are conserved, however MD simulations reveal ligand-specific effects on interaction dynamics Overlay of the four consensus cryo-EM static structures revealed very similar backbone conformations of the intracellular face of receptor, with the greatest divergence for the ICLs (where modelled), and similar engagement with G s in all four peptide bound structures (Figure 8)
Life Sciences, 51(13), 1049-1056.
This mutation also results in a CPT1A protein that is less sensitive for the inhibitory effect of malonyl-CoA on CPT1A under fed conditions, resulting in a 34 times higher activity of CPT1A compared to wild type [91,92,93]
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