Fig. 1: Structure of human p97 ATPase and designed triazole inhibitors used in this study. | Communications Chemistry

Fig. 1: Structure of human p97 ATPase and designed triazole inhibitors used in this study.

From: Mechanism of allosteric inhibition of human p97/VCP ATPase and its disease mutant by triazole inhibitors

Fig. 1

a Primary structure of human p97 ATPase. Location of the pathogenic mutation R155H (blue) and arginine fingers of D1 (R359, R362) and D2 domains (R635, R638) are labeled. α/β and α subdomains of the D1 and D2 ATPase domains are underlined. Highlighted regions (pink; D1 α and D2 α/β subdomains) are the domains that interact with the triazole-based inhibitors. b Structure of wild-type p97 with ADP and the triazole-based inhibitor bound (PDB code: 8UV2). The N-terminal (NTD), D1, D2, and linker domains are in green, orange, orange-red, and purple, respectively. Bound nucleotides and the triazole-based inhibitor are shown in space-filling representation in light and medium blue, respectively. The helices of the D2 domain are labeled. c Chemical structures of the lead compounds for p97 ATPase: NSC799462, NSC804515, NSC819701, NMS-873, and UPCDC30766.

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