7s13
From Proteopedia
Crystal structure of Fab in complex with mouse CD96 dimer
Structural highlights
FunctionTACT_MOUSE May be involved in adhesive interactions of activated T and NK cells during the late phase of the immune response. Promotes NK cell-target adhesion by interacting with PVR present on target cells. May function at a time after T and NK cells have penetrated the endothelium using integrins and selectins, when they are actively engaging diseased cells and moving within areas of inflammation (By similarity). Publication Abstract from PubMedThe 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. Antibody blockade of CD96 by distinct molecular mechanisms.,Lee PS, Chau B, Barman I, Bee C, Jashnani A, Hogan JM, Aguilar B, Dollinger G, Rajpal A, Strop P MAbs. 2021 Jan-Dec;13(1):1979800. doi: 10.1080/19420862.2021.1979800. PMID:34595996[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. Loading citation details.. Citations No citations found See AlsoReferences
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Categories: Large Structures | Mus musculus | Rattus | Barman I | Lee PS | Strop P
