View source for Basigin

<StructureSection load='4u0q' size='340' side='right' caption='Human basigin (green) complex with Plasmodium falciparum reticulocyte binding protein 5 (cyan) (PDB code [[4u0q]])' scene='10/1043826/Cv/2'>

== 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<ref>PMID:26684586</ref>.  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<ref>PMID:21536654</ref>.

== Relevance ==

Basigin is involved in regulation of glycolysis and thus in development of malignant tumors and T-cell-mediated immunological disorders<ref>PMID:35844594</ref>. 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 <scene name='10/1043826/Cv/3'>N-terminal</scene> and <scene name='10/1043826/Cv/5'>C-terminal domains</scene> as well as via the 2 domains' linker His102.  In addition, the structure shows several hydrophobic interactions between the two proteins<ref>PMID:25132548</ref>.

== Basigin 3D structures ==
[[3D structures of basigin]]

</StructureSection>
== References ==
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