Your browser doesn't support javascript.
loading
Preliminary crystallographic characterization of ricin agglutinin.
Sweeney, E C; Tonevitsky, A G; Temiakov, D E; Agapov, I I; Saward, S; Palmer, R A.
Affiliation
  • Sweeney EC; Department of Crystallography, Birkbeck College, University of London, United Kingdom.
Proteins ; 28(4): 586-9, 1997 Aug.
Article in En | MEDLINE | ID: mdl-9261874
The quaternary structure of ricin agglutinin (RCA) has been determined by x-ray crystallography. The refined structure of ricin proved to be a successful search model using the molecular replacement method of phase determination. RCA forms an elongated molecule of dimensions 120 A x 60 A x 40 A with two A chains at the center and a B chain at each end. The A chains are covalently associated via a disulfide bridge between Cys 156 of both chains. Additional contacts at residues 114-5 stabilize the dimer interface. The covalent association of RCAA chains was confirmed by gel filtration under reducing and nonreducing conditions.
Subject(s)
Search on Google
Collection: 01-internacional Database: MEDLINE Main subject: Protein Conformation / Plant Lectins / Lectins Language: En Journal: Proteins Journal subject: BIOQUIMICA Year: 1997 Document type: Article Affiliation country: Reino Unido Country of publication: Estados Unidos
Search on Google
Collection: 01-internacional Database: MEDLINE Main subject: Protein Conformation / Plant Lectins / Lectins Language: En Journal: Proteins Journal subject: BIOQUIMICA Year: 1997 Document type: Article Affiliation country: Reino Unido Country of publication: Estados Unidos