Fig. 1: Cryo-EM structure of hEP in the inactive state. | Nature Communications

Fig. 1: Cryo-EM structure of hEP in the inactive state.

From: Cryo-EM structures reveal the activation and substrate recognition mechanism of human enteropeptidase

Fig. 1: Cryo-EM structure of hEP in the inactive state.The alternative text for this image may have been generated using AI.

a Domains of hEP. Numbers indicate the N- or C-terminus positions of the domains in the amino acid sequence. The unexpressed domains (TM and SEA), as well as the flexible domains with a lower resolution (LDLR, CUB, and MAM), were colored in grey, CUB2 domain in pink, LDLR2 domain in light green, SRCR domain in orange, and the peptidase domain in dodger blue. This domain color scheme was used throughout this study. SEA: Sea urchin sperm protein, Enteropeptidase, and Agrin; MAM: meprin-like domain; SRCR: Scavenger Receptor Cysteine-rich Repeat; LDLR: Low-Density Lipoprotein Receptor; CUB: Complement, Urchin embryonic growth factor, and Bone morphogenetic protein-1. b Cryo-EM reconstruction of inactive hEP. The reconstruction is a composite map generated from the locally refined hEP-core and the low-resolution region of hEP-complete. The domain color scheme follows that in (a). Unless otherwise stated, the same domain color scheme is applied to all figures. c Structural model of the inactive hEP, with the map displayed as semi-transparent. The nine detected N-linked glycans are shown as stick atomic models, and the amino acid residues to which they are covalently attached are labeled. LCM: LDLR, CUB, and MAM domains.

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