7T99
Crystal structure of engineered CYS-CYS fab dimer CL-205 (LC25)
Summary for 7T99
| Entry DOI | 10.2210/pdb7t99/pdb |
| Descriptor | FAB Heavy Chain, FAB Light Chain, PHOSPHATE ION, ... (4 entities in total) |
| Functional Keywords | immune system |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 8 |
| Total formula weight | 191499.39 |
| Authors | |
| Primary citation | Yin, Y.,Romei, M.G.,Sankar, K.,Pal, L.R.,Hoi, K.H.,Yang, Y.,Leonard, B.,De Leon Boenig, G.,Kumar, N.,Matsumoto, M.,Payandeh, J.,Harris, S.F.,Moult, J.,Lazar, G.A. Antibody interfaces revealed through structural mining. Comput Struct Biotechnol J, 20:4952-4968, 2022 Cited by PubMed Abstract: Antibodies are fundamental effectors of humoral immunity, and have become a highly successful class of therapeutics. There is increasing evidence that antibodies utilize transient homotypic interactions to enhance function, and elucidation of such interactions can provide insights into their biology and new opportunities for their optimization as drugs. Yet the transitory nature of weak interactions makes them difficult to investigate. Capitalizing on their rich structural data and high conservation, we have characterized all the ways that antibody fragment antigen-binding (Fab) regions interact crystallographically. This approach led to the discovery of previously unrealized interfaces between antibodies. While diverse interactions exist, β-sheet dimers and variable-constant elbow dimers are recurrent motifs. Disulfide engineering enabled interactions to be trapped and investigated structurally and functionally, providing experimental validation of the interfaces and illustrating their potential for optimization. This work provides first insight into previously undiscovered oligomeric interactions between antibodies, and enables new opportunities for their biotherapeutic optimization. PubMed: 36147680DOI: 10.1016/j.csbj.2022.08.048 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.65 Å) |
Structure validation
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