Structure of the Anti-C60 Fullerene Antibody Fab Fragment: Structural Determinants of Fullerene Binding

Autor:	Em, Osipov, Od, Hendrickson, Tv, Tikhonova, Av, Zherdev, On, Solopova, Pg, Sveshnikov, Bb, Dzantiev, Vladimir Popov
Rok vydání:	2019
Předmět:	molecular modeling fullerene antibodies Molecular Biology Research Article X-ray analysis
Zdroj:	Acta Naturae Europe PubMed Central
ISSN:	2075-8251
Popis:	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 π-π 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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::772ef5b34033f9a35334bb4db5a3d76a https://pubmed.ncbi.nlm.nih.gov/31024749 Zobrazit plný text záznamu