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

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TitleThe predicted structure of immunoglobulin D1.3 and its comparison with the crystal structure.
Publication TypeJournal Article
Year of Publication1986
AuthorsChothia, C, Lesk, AM, Levitt, M, Amit, AG, Mariuzza, RA, Phillips, SE, Poljak, RJ
JournalScience
Volume233
Issue4765
Pagination755-8
Date Published1986 Aug 15
ISSN0036-8075
KeywordsAmino Acid Sequence, Animals, Antibodies, Monoclonal, Antigen-Antibody Complex, Chickens, Egg White, Female, Immunoglobulin Fab Fragments, Immunoglobulin G, Immunoglobulin Heavy Chains, Immunoglobulin Light Chains, Immunoglobulin Variable Region, Models, Molecular, Muramidase, Protein Conformation
Abstract

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.

Alternate JournalScience
PubMed ID3090684
Grant ListGM25435 / GM / NIGMS NIH HHS / United States