Function
Basigin or CD147 or EMMPRIN is a transmembranal glycoprotein which is a receptor for a variety of proteins and is expressed by tumor cells[1]. 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[2].
Relevance
Basigin is involved in regulation of glycolysis and thus in development of malignant tumors and T-cell-mediated immunological disorders[3]. 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 and as well as via the 2 domains' linker His102. In addition, the structure shows several hydrophobic interactions between the two proteins[4].
Basigin 3D structures
3D structures of basigin