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Structure of Galactose Binding lectin from Champedak (CGB) with Gal(beta)1,3-GalNacStructure of Galactose Binding lectin from Champedak (CGB) with Gal(beta)1,3-GalNac
Structural highlights
Function[LECA_ARTIN] D-galactose-specific lectin, binds the T-antigen structure Gal-beta1,3-GalNAc (Thomsen-Friedenreich-antigen-specific lectin). Potent and selective stimulant of distinct T- and B-cell functions. Shows a unique ability to specifically recognize IgA-1 from human serum. [LECB4_ARTIN] D-galactose-specific lectin, binds the T-antigen structure Gal-beta1,3-GalNAc (Thomsen-Friedenreich-antigen-specific lectin). Potent and selective stimulant of distinct T- and B-cell functions. Shows a unique ability to specifically recognize IgA-1 from human serum (By similarity). Publication Abstract from PubMedGalactose-binding and mannose-binding lectins from the champedak fruit, which is native to South-east Asia, exhibit useful potential clinical applications. The specificity of the two lectins for their respective ligands allows the detection of potential cancer biomarkers and monitoring of the glycosylated state of proteins in human serum and/or urine. To fully understand and expand the use of these natural proteins, their complete sequences and crystal structures are presented here, together with details of sugar binding. Structures and binding specificity of galactose- and mannose-binding lectins from champedak: differences from jackfruit lectins.,Gabrielsen M, Abdul-Rahman PS, Othman S, Hashim OH, Cogdell RJ Acta Crystallogr F Struct Biol Commun. 2014 Jun;70(Pt 6):709-16. doi:, 10.1107/S2053230X14008966. Epub 2014 May 24. PMID:24915077[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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