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The three-dimensional structure of ricin at 2.8 A
Journal of Biological Chemistry
The x-ray crystallographic structure of the heterodimeric plant toxin ricin has been determined at 2.8-A resolution. The A chain enzyme is a globular protein with extensive secondary structure and a reasonably prominent cleft assumed to be the active site. The B chain lectin folds into two topologically similar domains, each binding lactose in a shallow cleft. In each site a glutamine residue forms a hydrogen bond to the OH-4 of galactose, accounting for the epimerimic specificity of binding.pmid:3558397 fatcat:4xmwhdq47bbcbjixww2wt7lbs4