4R6R

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

Summary for 4R6R

• Entry DOI: 10.2210/pdb4r6r/pdb
• Related: 1JAC 1KU8 1M26 1UGW 1UGY 1UH0 4R6N 4R6O 4R6P 4R6Q
• Descriptor: Agglutinin alpha chain, Agglutinin beta-3 chain, 4-nitrophenyl beta-D-galactopyranoside, ... (6 entities in total)
• Functional Keywords: galactose specific lectin, beta-prism i fold, post translational proteolysis, t-antigen binding protein, plant lectins, galactose and sugar binding protein, sugar binding protein
• Biological source: Artocarpus integer (campedak,chempedak); More
• Total number of polymer chains: 8
• Total formula weight: 68055.12

Authors

Abhinav, K.V.,Sharma, K.,Swaminathan, C.P.,Surolia, A.,Vijayan, M. (deposition date: 2014-08-26, release date: 2015-02-18, Last modification date: 2023-11-08)

Primary citation

Abhinav, K.V.,Sharma, K.,Swaminathan, C.P.,Surolia, A.,Vijayan, M.
Jacalin-carbohydrate interactions: distortion of the ligand molecule as a determinant of affinity.
Acta Crystallogr.,Sect.D, 71:324-331, 2015

PubMed Abstract: 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 β-galactosides for jacalin compared with α-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 β-galactosides. The difference in energy, and therefore in affinity, is caused by a distortion of the sugar ring in β-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.

PubMed: 25664742
DOI: 10.1107/S139900471402553X

Experimental method

X-RAY DIFFRACTION (1.38 Å)