4r6r
From Proteopedia
Jacalin-carbohydrate interactions. Distortion of the ligand as a determinant of affinity.
Structural highlights
FunctionLECA_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. Publication Abstract from PubMedJacalin is among the most thoroughly studied lectins. Its carbohydrate-binding site has also been well characterized. It has been postulated that the lower affinity of beta-galactosides for jacalin compared with alpha-galactosides is caused by steric interactions of the substituents in the former with the protein. This issue has been explored energetically and structurally using different appropriate carbohydrate complexes of jacalin. It turns out that the earlier postulation is not correct. The interactions of the substituent with the binding site remain essentially the same irrespective of the anomeric nature of the substitution. This is achieved through a distortion of the sugar ring in beta-galactosides. The difference in energy, and therefore in affinity, is caused by a distortion of the sugar ring in beta-galactosides. The elucidation of this unprecedented distortion of the ligand as a strategy for modulating affinity is of general interest. The crystal structures also provide a rationale for the relative affinities of the different carbohydrate ligands for jacalin. Jacalin-carbohydrate interactions: distortion of the ligand molecule as a determinant of affinity.,Abhinav KV, Sharma K, Swaminathan CP, Surolia A, Vijayan M Acta Crystallogr D Biol Crystallogr. 2015 Feb;71(Pt 2):324-31. doi:, 10.1107/S139900471402553X. Epub 2015 Jan 23. PMID:25664742[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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