Basigin

spinqualitylabelsall models Human basigin (green) complex with Plasmodium falciparum reticulocyte binding protein 5 (grey) (PDB code 4u0q) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Basigin or CD147 or EMMORIN is a transmembranal glycoprotein which is a receptor for a variety of proteins and is expressed by tumor cells. Basigin has several isoforms and contains immunoglobulin-like domains (Ig-like). Alternative splicing of basigin results in 4 different isoforms. Basigin-2 is the most predominant form and contains 2 Ig-like domains. Basigin-1 contains 3 Ig-like domains, basigin-3 contains 1 Ig-like domain. Relevance Basigin is involved in regulation of glycolysis and thus in development of malignant tumors and T-cell-mediated immunological disorders. Hence, basigin has been termed a cancer-associated biomarker and serves as a target for cancer therapy. Structural highlights The 3D structure of the complex between basigin and the malaria causing Plasmodium falciparum erythrocyte invading protein reticulocyte binding protein 5 (RH5) shows the N-terminal and C-terminal domains of basigin. RH5 and basigin interact via various hydrogen bonds in both the N-terminal and C-terminal domains as well as via the 2 domains' linker His102. In addition, the structure shows several hydrophobic interactions between the two proteins. Basigin 3D structures 3D structures of basigin

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Michal Harel, Alexander Berchansky