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Fig. 4 | Journal of Translational Medicine

Fig. 4

From: Expanding the phenotypic spectrum of mutations in LRP2: a novel candidate gene of non-syndromic familial comitant strabismus

Fig. 4

Schematic structural of LRP2/megalin and predicted crystal structural models of the wild-type and mutant. a Megalin is composed of a large extracellular domain, a single transmembrane domain, and a short cytoplasmic domain. The extracellular domain harbors four cysteine-rich complement-type ligand binding repeats, which are separated from each other by β-propellers and EGF-like repeats. b-d Crystal structures of wild-type human LRP2 and mutant human LRP2 carrying p.Q112R. c The mutation spot is highlighted red. D, The 112 residue glutamine is replaced by arginine. e–g Crystal structures of wild-type and mutant human LRP2 carrying p.D2425G. e The mutated residue is indicated in green. Amino acids interacted with residue 2425, including Tyr2426, Tyr2434, Phe2473, and Asn2641, are indicated. g The hydrogen bond between residue 2425 and Tyr2434, Tyr2426, Phe2473, as well Asn2641 are eliminated upon the change from wild-type aspartic to mutant glycine

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