6H3H
Fab fragment of antibody against fullerene C60
Summary for 6H3H
| Entry DOI | 10.2210/pdb6h3h/pdb |
| Descriptor | Anti-fullerene antibody Fab fragment Heavy chain, Anti-fullerene antibody Fab fragment Light chain, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | antibody fab fullerene c60, immune system |
| Biological source | Mus musculus More |
| Total number of polymer chains | 4 |
| Total formula weight | 94754.92 |
| Authors | Osipov, E.M.,Tikhonova, T.V. (deposition date: 2018-07-18, release date: 2019-05-15, Last modification date: 2024-11-06) |
| Primary citation | Osipov, E.M.,Hendrickson, O.D.,Tikhonova, T.V.,Zherdev, A.V.,Solopova, O.N.,Sveshnikov, P.G.,Dzantiev, B.B.,Popov, V.O. Structure of the Anti-C60 Fullerene Antibody Fab Fragment: Structural Determinants of Fullerene Binding. Acta Naturae, 11:58-65, 2019 Cited by PubMed Abstract: The structure of the anti-C fullerene antibody Fab fragment (FabC) was solved by X-ray crystallography. The computer-aided docking of C into the antigen-binding pocket of FabC showed that binding of C to FabC 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 C. A fragment of the mobile CDR H3 loop located on the surface of FabC interferes with C binding in the antigen-binding site, thereby resulting in low antibody affinity for C. The structure of apo-FabC has been deposited with pdbid 6H3H. PubMed: 31024749PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.92 Å) |
Structure validation
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