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Fig. 1 | Journal of Biomedical Science

Fig. 1

From: Identifying N-linked glycan moiety and motifs in the cysteine-rich domain critical for N-glycosylation and intracellular trafficking of SR-AI and MARCO

Fig. 1

Modeled structure of the SRCR domain of human SR-AI and MACRO. a Schematic illustration of human MCRCO and SR-AI. The MARCO domains: cytoplamic domain (cyto), transmembrane domain (TM), spacer domain (Spa), coiled coil domain (coiled coil), triple-helical collagenous domain (collagenous), and cysteine-rich C-terminal domain (SRCR). The predicted N-glycosylation sides and amino acid sequence number was marked above and below the schematic illustration, respectively. b The structure of the SRCR domain of SR-AI and MACRO is composed of six β-strands (β1-6, yellow), one α-helix (α1, red), two 310 helices (η1, η2, blue), turns (indigo), and loops (gray). Disulfide bonds are shown in orange. The conformation folds with three β-strands (β1, β2, β3) at the N-terminal region followed by a short turn, α-helix (α1), and β4. Then, there are three long loops, located between β4 and β5, between β5 and η1, and between η1 and η2, ending with β6. Surface electrostatic potential representation of the SRCR domain of SR-AI and MACRO with basic (blue) and acidic (red) clusters. c Sequence alignment of human SR-AI and MACRO were displayed using ClustalW2 and ESPrip. The β-sheets are shown as arrows, and helixes are shown as a saw tooth pattern. Turns are marked as TT. The three pairs of disulfide bonds are labeled as numbers in green

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