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. 2021 Mar 21;476(8):2917–2942. doi: 10.1007/s11010-021-04107-3

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© The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2021

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Fig. 3 — A Human sMBL gene: The human sMBL gene with the corresponding mRNA and protein domains: The lengths of the four exons and three introns are indicated by the number of base pairs in the box of the figure. The mRNA encodes the various protein domains shown as signal peptide (SP), cysteine-rich region (CRR), collagen domain (CD), neck region (NR) (coiled-coil), and carbohydrate recognition domain (CRD) in the figure. The peptides self-associate into a homotrimer (structural subunit). Each peptide contains a lectin domain (gray) to bind the specific microbial carbohydrate motifs. Functional sMBL circulates in higher-order multimers: (tetramers, pentamers, and hexamers) [35]. B Human sMBL (or MBP) carbohydrate recognition domain (CRD) trimerizes through a triple α-helical coiled-coil [PDB:1HUP]. Courtesy Sheriff et al. [41]