Structural highlights
Function
[ITLN1_XENLA] Lectin that specifically recognizes microbial carbohydrate chains in a calcium-dependent manner (PubMed:26755729). Binds to microbial glycans that contain a terminal acyclic 1,2-diol moiety, including beta-linked D-galactofuranose (beta-Galf) and D-phosphoglycerol-modified glycans (PubMed:26755729). Binds to S.pneumoniae serotypes with glycans that contain beta-linked D-galactofuranose (beta-Galf) and with D-phosphoglycerol-modified glycans (PubMed:26755729). Can bind a variety of monosaccharides (in vitro) (PubMed:15537792). Probably plays a role in the defense system against microorganisms (Probable).[1] [2]
References
- ↑ Nagata S. Isolation, characterization, and extra-embryonic secretion of the Xenopus laevis embryonic epidermal lectin, XEEL. Glycobiology. 2005 Mar;15(3):281-90. doi: 10.1093/glycob/cwi010. Epub 2004 Nov, 10. PMID:15537792 doi:http://dx.doi.org/10.1093/glycob/cwi010
- ↑ Wangkanont K, Wesener DA, Vidani JA, Kiessling LL, Forest KT. Structures of Xenopus embryonic epidermal lectin reveal a conserved mechanism of microbial glycan recognition. J Biol Chem. 2016 Jan 11. pii: jbc.M115.709212. PMID:26755729 doi:http://dx.doi.org/10.1074/jbc.M115.709212