Crystallization and preliminary X-ray diffraction data of an anti-angiotensin II Fab and of the peptide-Fab complex

K. C. Garcia, P. Ronco, P. J. Verroust, L. M. Amzel

Research output: Contribution to journalArticle

Abstract

mAb-131 is a monoclonal antibody that binds with high affinity (K(a) = 7.4 x 109 M-1) to the 8-residue peptide hormone angiotensin II, the major effector of the renin/angiotensin system. mAb-131 is a member of a well characterized idiotypic antibody network since it was raised as an anti-anti-idiotype of an antibody raised against angiotensin II. mAb-131 Fabs prepared with papain contain four major charge isoforms that can be separated by pH gradient elution from an anion-exchange column. Diffraction quality isomorphous crystals of two of the isoforms and of the Fab·peptide complexes have been grown. The crystals diffract to 3.5 Å resolution, are tetragonal, space group P41 (or P43) with cell dimensions a = b = 78.6 Å, c = 25.2 Å, and have two Fab molecules per asymmetric unit. By using a different buffer, a second crystal form has been grown which diffracts to 3.3 Å. It also belongs to space group P41 (or P43) but has cell dimensions of a = b = 109.6 Å and c = 125.2 Å. Knowledge of the three-dimensional structure of this Fab and of the peptide·Fab complex will give insight into two problems: 1) the recognition of small peptide hormones (which exist as random coils in solution) with high affinity by proteins, and 2) the nature of conservation of antibody combining sites in idiotypic networks.

Original languageEnglish (US)
Pages (from-to)20463-20466
Number of pages4
JournalJournal of Biological Chemistry
Volume264
Issue number34
StatePublished - Dec 20 1989

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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