Three-dimensional structure of an antibody-antigen complex.

S. Sheriff, E. W. Silverton, E. A. Padlan, G. H. Cohen, S. J. Smith-Gill, B. C. Finzel, D. R. Davies

Research output: Contribution to journalArticlepeer-review

597 Scopus citations

Abstract

We have determined the three-dimensional structure of two crystal forms of an antilysozyme Fab-lysozyme complex by x-ray crystallography. The epitope on lysozyme consists of three sequentially separated subsites, including one long, nearly continuous, site from Gln-41 through Tyr-53 and one from Gly-67 through Pro-70. Antibody residues interacting with lysozyme occur in each of the six complementarity-determining regions and also include one framework residue. Arg-45 and Arg-68 form a ridge on the surface of lysozyme, which binds in a groove on the antibody surface. Otherwise the surface of interaction between the two proteins is relatively flat, although it curls at the edges. The surface of interaction is approximately 26 X 19 A. No water molecules are found in the interface. The positive charge on the two arginines is complemented by the negative charge of Glu-35 and Glu-50 from the heavy chain of the antibody. The backbone structure of the antigen, lysozyme, is mostly unperturbed, although there are some changes in the epitope region, most notably Pro-70. One side chain not in the epitope, Trp-63, undergoes a rotation of approximately 180 degrees about the C beta--C gamma bond. The Fab elbow bends in the two crystal forms differ by 7 degrees.

Original languageEnglish (US)
Pages (from-to)8075-8079
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume84
Issue number22
DOIs
StatePublished - Nov 1987

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