Basigin: Difference between revisions

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<StructureSection load='4u0q' size='340' side='right' caption='Caption for this structure' scene=''>
<StructureSection load='4u0q' size='340' side='right' caption='Human basigin (green) complex with Plasmodium falciparum reticulocyte binding protein 5 (grey) (PDB code [[4u0q]])' scene=''>


== Function ==
== Function ==

Revision as of 11:02, 1 May 2024


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[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].

Disease

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

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.


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

Drag the structure with the mouse to rotate

ReferencesReferences

  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

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

Michal Harel, Alexander Berchansky