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 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

Human basigin (green) complex with Plasmodium falciparum reticulocyte binding protein 5 (cyan) (PDB code 4u0q)

Drag the structure with the mouse to rotate

ReferencesReferences

↑ Muramatsu T. Basigin (CD147), a multifunctional transmembrane glycoprotein with various binding partners. J Biochem. 2016 May;159(5):481-90. PMID:26684586 doi:10.1093/jb/mvv127
↑ Liao CG, Kong LM, Song F, Xing JL, Wang LX, Sun ZJ, Tang H, Yao H, Zhang Y, Wang L, Wang Y, Yang XM, Li Y, Chen ZN. Characterization of basigin isoforms and the inhibitory function of basigin-3 in human hepatocellular carcinoma proliferation and invasion. Mol Cell Biol. 2011 Jul;31(13):2591-604. PMID:21536654 doi:10.1128/MCB.05160-11
↑ Xu Y, Chen Y, Zhang X, Ma J, Liu Y, Cui L, Wang F. Glycolysis in Innate Immune Cells Contributes to Autoimmunity. Front Immunol. 2022 Jul 1;13:920029. PMID:35844594 doi:10.3389/fimmu.2022.920029
↑ Wright KE, Hjerrild KA, Bartlett J, Douglas AD, Jin J, Brown RE, Illingworth JJ, Ashfield R, Clemmensen SB, de Jongh WA, Draper SJ, Higgins MK. Structure of malaria invasion protein RH5 with erythrocyte basigin and blocking antibodies. Nature. 2014 Aug 17. doi: 10.1038/nature13715. PMID:25132548 doi:http://dx.doi.org/10.1038/nature13715

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

[1] Muramatsu T. Basigin (CD147), a multifunctional transmembrane glycoprotein with various binding partners. J Biochem. 2016 May;159(5):481-90. PMID:26684586 doi:10.1093/jb/mvv127

[2] Liao CG, Kong LM, Song F, Xing JL, Wang LX, Sun ZJ, Tang H, Yao H, Zhang Y, Wang L, Wang Y, Yang XM, Li Y, Chen ZN. Characterization of basigin isoforms and the inhibitory function of basigin-3 in human hepatocellular carcinoma proliferation and invasion. Mol Cell Biol. 2011 Jul;31(13):2591-604. PMID:21536654 doi:10.1128/MCB.05160-11

[3] Xu Y, Chen Y, Zhang X, Ma J, Liu Y, Cui L, Wang F. Glycolysis in Innate Immune Cells Contributes to Autoimmunity. Front Immunol. 2022 Jul 1;13:920029. PMID:35844594 doi:10.3389/fimmu.2022.920029

[4] Wright KE, Hjerrild KA, Bartlett J, Douglas AD, Jin J, Brown RE, Illingworth JJ, Ashfield R, Clemmensen SB, de Jongh WA, Draper SJ, Higgins MK. Structure of malaria invasion protein RH5 with erythrocyte basigin and blocking antibodies. Nature. 2014 Aug 17. doi: 10.1038/nature13715. PMID:25132548 doi:http://dx.doi.org/10.1038/nature13715

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