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Science 15 August 1986:
Vol. 233. no. 4765, pp. 755 - 758
DOI: 10.1126/science.3090684
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Articles

Science, Vol 233, Issue 4765, 755-758
Copyright © 1986 by American Association for the Advancement of Science

articles

The predicted structure of immunoglobulin D1.3 and its comparison with the crystal structure

C Chothia, AM Lesk, M Levitt, AG Amit, RA Mariuzza, SE Phillips, and RJ Poljak

Predictions of the structures of the antigen-binding domains of an antibody, recorded before its experimental structure determination and tested subsequently, were based on comparative analysis of known antibody structures or on conformational energy calculations. The framework, the relative positions of the hypervariable regions, and the folds of four of the hypervariable loops were predicted correctly. This portion includes all residues in contact with the antigen, in this case hen egg white lysozyme, implying that the main chain conformation of the antibody combining site does not change upon ligation. The conformations of three residues in each of the other two hypervariable loops are different in the predicted models and the experimental structure.


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