2x2s

Structural highlights

Function

AGGL_SCLSC Lectin that primarily recognizes glycans with a non-reducing terminal N-acetylgalactosamine (GalNAc), with a preference for the alpha- over the beta-anomer. Can also bind non-reducing terminal galactose (Gal) residues but with a lower affinity. Strongly interacts with glycolipid type glycans with terminal non-reducing Gal or GalNAc but fails to bind sialylated or fucosylated forms of the same glycans. Strongly interacts with galactosylated N-glycans, displaying highest affinity for alpha-1-3 branched mono-antennary N-glycans but also binding to multi-antennary glycans.^{[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.

See Also

• Agglutinin 3D structures

References

1. ↑ Candy L, Van Damme EJ, Peumans WJ, Menu-Bouaouiche L, Erard M, Rougé P. Structural and functional characterization of the GalNAc/Gal-specific lectin from the phytopathogenic ascomycete Sclerotinia sclerotiorum (Lib.) de Bary. Biochem Biophys Res Commun. 2003 Aug 22;308(2):396-402. PMID:12901882 doi:10.1016/s0006-291x(03)01406-2
2. ↑ Van Damme EJ, Nakamura-Tsuruta S, Hirabayashi J, Rougé P, Peumans WJ. The Sclerotinia sclerotiorum agglutinin represents a novel family of fungal lectins remotely related to the Clostridium botulinum non-toxin haemagglutinin HA33/A. Glycoconj J. 2007 Apr;24(2-3):143-56. PMID:17294128 doi:10.1007/s10719-006-9022-z
3. ↑ Sulzenbacher G, Roig-Zamboni V, Peumans WJ, Rouge P, Van Damme EJ, Bourne Y. Crystal structure of the GalNAc/Gal-specific agglutinin from the phytopathogenic ascomycete Sclerotinia sclerotiorum reveals novel adaptation of a beta-trefoil domain. J Mol Biol. 2010 Jul 23;400(4):715-23. Epub 2010 May 24. PMID:20566411 doi:10.1016/j.jmb.2010.05.038