Structural highlights
Publication Abstract from PubMed
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 pi-pi 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.
Structure of the Anti-C60 Fullerene Antibody Fab Fragment: Structural Determinants of Fullerene Binding.,Osipov EM, Hendrickson OD, Tikhonova TV, Zherdev AV, Solopova ON, Sveshnikov PG, Dzantiev BB, Popov VO Acta Naturae. 2019 Jan-Mar;11(1):58-65. PMID:31024749[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Osipov EM, Hendrickson OD, Tikhonova TV, Zherdev AV, Solopova ON, Sveshnikov PG, Dzantiev BB, Popov VO. Structure of the Anti-C60 Fullerene Antibody Fab Fragment: Structural Determinants of Fullerene Binding. Acta Naturae. 2019 Jan-Mar;11(1):58-65. PMID:31024749
