7S13

Crystal structure of Fab in complex with mouse CD96 dimer

7S13 の概要

• エントリーDOI: 10.2210/pdb7s13/pdb
• 分子名称: Fab heavy chain, Fab light chain, T-cell surface protein tactile, ... (7 entities in total)
• 機能のキーワード: immunoglobulin, checkpoint, antibody, complex, immune system
• 由来する生物種: Rattus; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 124575.74

構造登録者

Lee, P.S.,Barman, I.,Strop, P. (登録日: 2021-08-31, 公開日: 2021-10-20, 最終更新日: 2024-10-23)

主引用文献

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

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: 34595996
DOI: 10.1080/19420862.2021.1979800

実験手法

X-RAY DIFFRACTION (2.12 Å)