Crystal structure of a constitutive active mutant of adenosine A2A receptor

Cui, M.; Zhou, Q.; Xu, Y.; Weng, Y.; Yao, D.; Zhao, S.; Song, G.

doi:10.1107/S2052252522001907

Figure 4
Conformational dynamics of the intracellular part of TM6 during MD simulations. (a) Structural comparison of the intracellular half of TM6 between a representative MD snapshot and the released structure of A_2AAR in different states. Inactive, intermediate and active conformations are colored in orange, magenta and green, respectively (Liu et al., 2012

; Xu et al., 2011

; Carpenter et al., 2016

). All other TMs and ICLs are omitted for clarity. (b) Movements of TM6 during MD simulations: top, minimum distance between the charged non-hydrogen atoms of Arg102^3.50 and Glu228^6.30; middle, the Cα distance between Arg102^3.50 and the intracellular tip of TM6 (Thr224^6.26); bottom, the SASA of G-protein binding sites, which consists of Arg102^3.50, Ala105^3.53, Ile106^3.54, Ile200^5.61, Ala203^5.64, Ser234^6.36 and Leu235^6.37. The interface areas were calculated by FreeSASA (Mitternacht, 2016

). Dashed horizontal lines indicate values for the released structure of A_2AAR in different states (inactive state, orange; intermediate state, magenta; active state, green).

IUCrJ

Volume 9| Part 3| May 2022| Pages 333-341

ISSN: 2052-2525

https://doi.org/10.1107/S2052252522001907

BIOLOGY | MEDICINE

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