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| Item Type: | Article |
|---|---|
| Title: | A complex water network contributes to high-affinity binding in an antibody-antigen interface |
| Creators Name: | Marino, S.F., Olal, D. and Daumke, O. |
| Abstract: | This data article presents an analysis of structural water molecules in the high affinity interaction between a potent tumor growth inhibiting antibody (fragment), J22.9-xi, and the tumor marker antigen CD269 (B cell maturation antigen, BCMA). The 1.89 {Angstrom} X-ray crystal structure shows exquisite details of the binding interface between the two molecules, which comprises relatively few, mostly hydrophobic, direct contacts but many indirect interactions over solvent waters. These are partly or wholly buried in, and therefore part of, the interface. A partial description of the structure is included in an article on the tumor inhibiting effects of the antibody: "Potent anti-tumor response by targeting B cell maturation antigen (BCMA) in a mouse model of multiple myeloma", Mol. Oncol. 9 (7) (2015) pp. 1348–58. |
| Keywords: | Crystal Structure, Fab Fragment, BCMA, Binding Interface, High Affinity, Water Molecules, Animals, Mice |
| Source: | Data in Brief |
| ISSN: | 2352-3409 |
| Publisher: | Elsevier |
| Volume: | 6 |
| Page Range: | 394-397 |
| Date: | March 2016 |
| Official Publication: | https://doi.org/10.1016/j.dib.2015.12.023 |
| PubMed: | View item in PubMed |
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