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Crystallographic refinement of the three-dimensional structure of the FabD1.3-lysozyme complex at 2.5-A resolution

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Fischmann, T.O., Bentley, G.A., Bhat, T.N., Boulot, G., Mariuzza, R.A., Phillips, S.E., Tello, D., Poljak, R.J.·1991·Journal of Biological Chemistry

Abstract

The three-dimensional crystal structure of the complex between the Fab from the monoclonal anti-lysozyme antibody D1.3 and the antigen, hen egg white lysozyme, has been refined by crystallographic techniques using x-ray intensity data to 2.5-A resolution. The antibody contacts the antigen with residues from all its complementarity determining regions. Antigen residues 18-27 and 117-125 form a discontinuous antigenic determinant making hydrogen bonds and van der Waals interactions with the antibody. Water molecules at or near the antigen-antibody interface mediate some contacts between antigen and antibody. The fine specificity of antibody D1.3, which does not bind (K alpha less than 10(5) M-1) avian lysozymes where Gln121 in the amino acid sequence is occupied by His, can be explained on the basis of the refined model.

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Metadata

Authors
Fischmann, T. O., Bentley, G. A., Bhat, T. N., Boulot, G., Mariuzza, R. A., Phillips, S. E., Tello, D., & Poljak, R. J.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1991-07
Volume
266
Issue
20
Pages
12915-12920
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1858317139
Cited by
174
References
0
FWCI
15.78
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Crystallographic refinement of the three-dimensional structure of the FabD1.3-lysozyme complex at 2.5-A resolution. https://app.cochat.ai/papers/10.1016/s0021-9258(18)98782-x
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Fischmann, T. O., Bentley, G. A., Bhat, T. N., Boulot, G., Mariuzza, R. A., Phillips, S. E., Tello, D., & Poljak, R. J. (1991). Crystallographic refinement of the three-dimensional structure of the FabD1.3-lysozyme complex at 2.5-A resolution. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)98782-x

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