The leucine-rich repeat (LRR) family of proteins, including LRG1, have been shown to be involved in protein-protein interaction, signal transduction, and cell adhesion and development. LRG1 is expressed during granulocyte differentiation.
Human LRG1 was isolated from human serum by Haupt and Baudner, 1977. By sequence analysis, Takahashi et al. (1985) determined that purified LRG1 protein has 312 amino acids and an experimentally determined molecular mass of 45 kD. The LRG1 polypeptide contains 1 galactosamine and 4 glucosamine oligosaccharides attached and has 2 intrachain disulfide bonds. Leucine comprises 66 of the 312 amino acids, and LRG1 contains at least 8 24-amino acid leucine-rich repeats.
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