%0 Journal Article
%T Structure of the Anti-C60 Fullerene Antibody Fab Fragment: Structural Determinants of Fullerene Binding
%A A. V. Zherdev
%A B. B. Dzantiev
%A E. M. Osipov
%A O. D. Hendrickson
%A O. N. Solopova
%A P. G. Sveshnikov
%A T. V. Tikhonova
%A V. O. Popov
%J Archive of "Acta Naturae".
%D 2019
%X The structure of the anti-C60 fullerene antibody Fab fragment (FabC60) was solved by X-ray crystallography. The computer-aided docking of C60 into the antigen-binding pocket of FabC60 showed that binding of C60 to FabC60 is governed by the enthalpy and entropy; namely, by ¦Ð-¦Ð stacking interactions with aromatic residues of the antigen-binding site and reduction of the solvent-accessible area of the hydrophobic surface of C60. A fragment of the mobile CDR H3 loop located on the surface of FabC60 interferes with C60 binding in the antigen-binding site, thereby resulting in low antibody affinity for C60. The structure of apo-FabC60 has been deposited with pdbid 6H3H
%K antibodies
%K fullerene
%K molecular modeling
%K X-ray analysis
%U https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6475864/