The three-dimensional structure of ricin at 2.8 A.

W. Montfort, J. E. Villafranca, A. F. Monzingo, S. R. Ernst, B. Katzin, E. Rutenber, N. H. Xuong, R. Hamlin, J. D. Robertus

Research output: Contribution to journalArticlepeer-review

351 Scopus citations


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. The interface between the A and B chains shows some hydrophobic contacts in which proline and phenylalanine side chains play a prominent role.

Original languageEnglish (US)
Pages (from-to)5398-5403
Number of pages6
JournalJournal of Biological Chemistry
Issue number11
StatePublished - Apr 15 1987

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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