NDLI: Modulation of antibody affinity by a non-contact residue.

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Modulation of antibody affinity by a non-contact residue.

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Modulation of antibody affinity by a non-contact residue.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Bruccoleri, R. E. Novotny, J. Sheriff, S. Haber, E. Jeffrey, P. D. Margolies, M. N. Schillbach, J. F. Near, R. I.
Description	Author Affiliation: Schillbach JF ( Program on Immunology, Harvard University Graduate School of Arts and Sciences, Cambridge, Massachusetts 02138.)
Abstract	Antibody LB4, produced by a spontaneous variant of the murine anti-digoxin monoclonal antibody 26-10, has an affinity for digoxin two orders of magnitude lower than that of the parent antibody due to replacement of serine with phenylalanine at position 52 of the heavy chain variable region (Schildbach, J.F., Panka, D.J., Parks, D.R., et al., 1991, J. Biol. Chem. 266, 4640-4647). To examine the basis for the decreased affinity, a panel of engineered antibodies with substitutions at position 52 was created, and their affinities for digoxin were measured. The antibody affinities decreased concomitantly with increasing size of the substituted side chains, although the shape of the side chains also influenced affinity. The crystal structure of the 26-10 Fab complexed with digoxin (P.D.J., R.K. Strong, L.C. Sieker, C. Chang, R.L. Campbell, G.A. Petsko, E.H., M.N.M., & S.S., submitted for publication) shows that the serine at heavy chain position 52 is not in contact with hapten, but is adjacent to a tyrosine at heavy chain position 33 that is a contact residue. The mutant antibodies were modeled by applying a conformational search procedure to position side chains, using the 26-10 Fab crystal structure as a starting point. The results suggest that each of the substituted side chains may be accommodated within the antibody without substantial structural rearrangement, and that none of these substituted side chains are able to contact hapten. These modeling results are consistent with the substituents at position 52 having only an indirect influence upon antibody affinity.(ABSTRACT TRUNCATED AT 250 WORDS)
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	2
Volume Number	2
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1993-02-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Antibodies, Monoclonal Genetics Antibody Affinity Immunology Binding Sites, Antibody Digoxin Animals Chemistry Cell Line Digoxigenin Mice Models, Molecular Molecular Sequence Data Mutagenesis, Site-directed Structure-activity Relationship Research Support, U.s. Gov't, Non-p.h.s. Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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