Structural highlights
Function
ABL_AGABI Lectin that recognizes O-linked galactose-beta-1,3-N-acetylgalactosamine, a disaccharide (Thomsen-Friedenreich antigen or T-disaccharide), present on cell surface glycoproteins. Can also bind galactose-beta-1,3-N-acetylglucosamine. Does not bind monosaccharides. Can be internalized by clathrin-coated vesicles after binding to surface glycoproteins. After internalization it inhibits nuclear import of nuclear localization signal dependent proteins. Inhibits proliferation of malignant cells without cytotoxicity for normal cells.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Presant CA, Kornfeld S. Characterization of the cell surface receptor for the Agaricus bisporus hemagglutinin. J Biol Chem. 1972 Nov 10;247(21):6937-45. PMID:4343164
- ↑ Yu L, Fernig DG, Smith JA, Milton JD, Rhodes JM. Reversible inhibition of proliferation of epithelial cell lines by Agaricus bisporus (edible mushroom) lectin. Cancer Res. 1993 Oct 1;53(19):4627-32. PMID:8402638
- ↑ Yu LG, Fernig DG, White MR, Spiller DG, Appleton P, Evans RC, Grierson I, Smith JA, Davies H, Gerasimenko OV, Petersen OH, Milton JD, Rhodes JM. Edible mushroom (Agaricus bisporus) lectin, which reversibly inhibits epithelial cell proliferation, blocks nuclear localization sequence-dependent nuclear protein import. J Biol Chem. 1999 Feb 19;274(8):4890-9. PMID:9988731
