5J4X

Structure of tetrameric jacalin complexed with Gal beta-(1,3) Gal-beta-OMe

Summary for 5J4X

• Entry DOI: 10.2210/pdb5j4x/pdb
• Related: 1JAC 1KU8 1KUJ 1M26 1UGW 1UGX 1UGY 1UH0 1UH1 1WS4 1WS5 4R6N 4R6O 4R6P 4R6Q 4R6R 5J50 5J51 5J52
• Descriptor: Agglutinin alpha chain, Agglutinin beta-3 chain, beta-D-galactopyranose-(1-3)-methyl beta-D-galactopyranoside, ... (6 entities in total)
• Functional Keywords: plant lectins and sugar binding protein, galactose specific lectin, beta-prism i fold, post translational proteolysis, t-antigen binding protein, reducing and non-reducing sugars, sugar binding protein
• Biological source: Artocarpus integer (Jack fruit); More
• Total number of polymer chains: 8
• Total formula weight: 67818.03

Authors

Abhinav, K.V.,Sharma, K.,Surolia, A.,Vijayan, M. (deposition date: 2016-04-01, release date: 2017-02-08, Last modification date: 2023-11-08)

Primary citation

Abhinav, K.V.,Sharma, K.,Surolia, A.,Vijayan, M.
Distortion of the ligand molecule as a strategy for modulating binding affinity: Further studies involving complexes of jacalin with beta-substituted disaccharides.
IUBMB Life, 69:72-78, 2017

PubMed Abstract: Crystal structures of jacalin in complex with GlcNAc β-(1,3) Gal-β-OMe and Gal β-(1,3) Gal-β-OMe have been determined. The binding of the ligands to jacalin is similar to that of analogous α-substituted disaccharides. However, the β-substituted β-(1,3) linked disaccharides get distorted at the anomeric center and the glycosidic linkage. The distortion results in higher internal energies of the ligands leading to lower affinity to the lectin. This confirms the possibility of using ligand distortion as a strategy for modulating binding affinity. Unlike in the case of β-substituted monosaccharides bound to jacalin, where a larger distortion at the anomeric center was observed, smaller distortions are distributed among two centers in the structures of the two β-substituted β-(1,3) linked disaccharides presented here. These disaccharides, like the unsubstituted and α-substituted counterparts, bind jacalin with the reducing Gal at the primary binding site, indicating that the lower binding affinity of β-substituted disaccharides is not enough to overcome the intrinsic propensity of Gal β-(1,3) Gal-based disaccharides to bind jacalin with the reducing sugar at the primary site. © 2017 IUBMB Life, 69(2):72-78, 2017.

PubMed: 28111895
DOI: 10.1002/iub.1593

Experimental method

X-RAY DIFFRACTION (1.65 Å)