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Figure 3
Conformational dynamics of the ligand-binding pocket in the MD simulations of WT A2AAR and its mutant I92N. (a), Structural comparison of the residues around Ile/Asn923.40 between a representative MD snapshot and the released structures of A2AAR in different states. Inactive (antagonist bound), intermediate (agonist bound) and active (both agonist and G-protein bound) A2AAR structures are colored in orange, magenta and green, respectively (Liu et al., 2012BB24; Xu et al., 2011BB40; Carpenter et al., 2016BB7). (b) Statistics of hydrogen bonds between Asn92 and its surrounding residues during the last 500 ns MD simulation of UK-432097-bound A2AAR mutant I92N. (c) Representative distances between Ile/Asn923.40 and its surrounding residues Cys1855.46, Trp2466.48 and Asn2807.45. Minimum distances were measured between non-hydrogen atoms for the selected two residues. Dashed horizontal lines indicate values for the released structure of A2AAR in different states (inactive state, orange; intermediate state, magenta; active state, green).

Volume 9| Part 3| May 2022| Pages 333-341
ISSN: 2052-2525