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. 2020 Mar 4;367(6485):1444–1448. doi: 10.1126/science.abb2762

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Copyright © 2020 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works

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Fig. 2 — (A) ACE2 dimerizes through two interfaces, the PD and the neck domain. The regions enclosed by the cyan and red dashed lines are illustrated in detail in (B) and (C), respectively. (B) The primary dimeric interface is through the neck domain in ACE2. Polar interactions are represented by red dashed lines. (C) A weaker interface between PDs of ACE2. The only interaction is between Gln¹³⁹ and Gln¹⁷⁵^′, which are highlighted as spheres. The polar residues that may contribute to the stabilization of Gln¹³⁹ are shown as sticks. (D) The PDs no longer contact each other in the open state. Single-letter abbreviations for the amino acid residues used in the figures are as follows: C, Cys; D, Asp; E, Glu; F, Phe; H, His; K, Lys; L, Leu; M, Met; N, Asn; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; and Y, Tyr.