7S13
Crystal structure of Fab in complex with mouse CD96 dimer
Summary for 7S13
| Entry DOI | 10.2210/pdb7s13/pdb |
| Descriptor | Fab heavy chain, Fab light chain, T-cell surface protein tactile, ... (7 entities in total) |
| Functional Keywords | immunoglobulin, checkpoint, antibody, complex, immune system |
| Biological source | Rattus More |
| Total number of polymer chains | 6 |
| Total formula weight | 124575.74 |
| Authors | Lee, P.S.,Barman, I.,Strop, P. (deposition date: 2021-08-31, release date: 2021-10-20, Last modification date: 2024-10-23) |
| Primary citation | Lee, P.S.,Chau, B.,Barman, I.,Bee, C.,Jashnani, A.,Hogan, J.M.,Aguilar, B.,Dollinger, G.,Rajpal, A.,Strop, P. Antibody blockade of CD96 by distinct molecular mechanisms. Mabs, 13:1979800-1979800, 2021 Cited by PubMed Abstract: The molecular interactions of mouse CD96 to CD155 ligand and to two surrogate antibodies have been investigated. Biophysical and structural studies demonstrate that CD96 forms a homodimer but assembles as 1:1 heterodimeric complexes with CD155 or with one of the surrogate antibodies, which compete for the same binding interface. In comparison, the other surrogate antibody binds across the mouse CD96 dimer and recognizes a quaternary epitope spanning both protomers to block exposure of the ligand-binding site. This study reveals different blocking mechanisms and modalities of these two antibodies and may provide insight into the functional effects of antibodies against CD96. PubMed: 34595996DOI: 10.1080/19420862.2021.1979800 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.12 Å) |
Structure validation
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