Basigin

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 C-terminal domains 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