Biochemical Properties | presence of seven putative
transmembrane domains; extended extracellular segment containing several adhesion
molecule structure motifs, and has been shown to interact with the human complement regulator,
decay-accelerating factor (DAF, CD55); human CD97 has an extended extracellular domain containing multiple epidermal growth factor (EGF)-like repeats, calcium-binding
sites and an Arg-Gly-Asp (RGD) motif; CD97 exists on the cell membrane as a processed heterodimer, consisting of an
extracellular a-subunit non-covalently linked to a seven-transmembrane b-subunit; |
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Bibliography | 1. Qian, Y. M., Haino, M., Kelly, K., & Song, W. C. (1999). Structural characterization of mouse CD97 and study of its specific interaction with the murine decay-accelerating factor (DAF, CD55). Immunology, 98(2), 303–311. https://doi.org/10.1046/j.1365-2567.1999.00859. 2. Wobus, M., Vogel, B., Schmücking, E., Hamann, J., & Aust, G. (2004). N-glycosylation of CD97 within the EGF domains is crucial for epitope accessibility in normal and malignant cells as well as CD55 ligand binding. International Journal of Cancer, 112(5), 815–822. https://doi.org/10.1002/ijc.20483. 3. Yang, L.-Y., Liu, X.-F., Yang, Y., Yang, L.-L., Liu, K.-W., Tang, Y.-B., … Huang, W. (2017). Biochemical features of the adhesion G protein-coupled receptor CD97 related to its auto-proteolysis and HeLa cell attachment activities. Acta Pharmacologica Sinica, 38(1), 56–68. https://doi.org/10.1038/aps.2016.89. |