4r6n

Jacalin-carbohydrate interactions. Distortion of the ligand as a determinant of affinity

spinqualitylabelsall models 4r6n, resolution 1.67Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4r6n is a 8 chain structure with sequence from Artocarpus integer. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.67Å Ligands: EDO, IPA, MBG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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. Publication Abstract from PubMed Jacalin 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Agglutinin 3D structures

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