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Crystallographic analysis of the interaction between cyclosporin A and the Fab fragment of a monoclonal antibody
Author(s) -
Vix Olivier,
Rees Bernard,
Thierry JeanClaude,
Altschuh Danièle
Publication year - 1993
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340150402
Subject(s) - monoclonal antibody , immunoglobulin fab fragments , resolution (logic) , chemistry , hypervariable region , molecular replacement , fragment (logic) , van der waals force , loop (graph theory) , antibody , stereochemistry , crystallography , complementarity determining region , crystal structure , molecule , biology , genetics , mathematics , computer science , organic chemistry , algorithm , combinatorics , artificial intelligence
The structure of the complex between cyclosporin A and the Fab fragment of a monoclonal antibody has been established by Crystallographic analysis to 2.65 Åresolution. The structure has been solved by molecular replacement using a composite Fab model. The current R ‐factor after refinement is 0.179 between 8 and 2.65Åresolution. The antibody is one among three known structures with long H3 loops. This loop conformation is observed for the first tune in the presence of the antigen. Residues from all six hypervariable loops interact with cyclosporin A. However, the 17 residues long loop H3 is the main contributor to the buried combining site area and to the van der Waals contacts made with cyclosporin A, with 52 and 63%, respectively, of the total contribution. © 1993 Wiley‐Liss, Inc.