Fig. 3: Interactions of the M1 region of helix V with helices III and IV in the closed and open forms of AdipoR1(A208). | Communications Biology

Fig. 3: Interactions of the M1 region of helix V with helices III and IV in the closed and open forms of AdipoR1(A208).

From: Human adiponectin receptor AdipoR1 assumes closed and open structures

Fig. 3: Interactions of the M1 region of helix V with helices III and IV in the closed and open forms of AdipoR1(A208).

Hydrophobic interactions of helix V in the closed form (molecule A) (a–c) and the open form (molecule C) (d–f). Val270 of helix V interacts with helix IV (a, d), and Phe271 of helix V interacts with helix IV (b, e) and helix III (c, f). Overall, the degrees of the hydrophobic interactions are much more intensive in the open form (d–f) than the closed form (a–c).

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