Osipov E M, Hendrickson O D, Tikhonova T V, Zherdev A V, Solopova O N, Sveshnikov P G, Dzantiev B B, Popov V O
Bach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, Leninsky Ave. 33, 119071, Moscow, Russia.
Russian Research Center of Molecular Diagnostics and Therapy, Simpheropolsky Blvd. 8, 113149, Moscow, Russia.
Acta Naturae. 2019 Jan-Mar;11(1):58-65.
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.
通过X射线晶体学解析了抗C富勒烯抗体Fab片段（FabC）的结构。将C与FabC的抗原结合口袋进行计算机辅助对接显示，C与FabC的结合受焓和熵的控制；也就是说，通过与抗原结合位点的芳香族残基的π-π堆积相互作用以及C疏水表面溶剂可及面积的减少。位于FabC表面的可移动互补决定区H3环片段干扰了抗原结合位点中C的结合，从而导致抗体对C的亲和力较低。无配体FabC的结构已存入蛋白质数据库，编号为6H3H。
