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Crystal structure and its bearing towards an understanding of key biological functions of EpCAM

Author

Listed:
  • Miha Pavšič

    (Faculty of Chemistry and Chemical Technology, University of Ljubljana)

  • Gregor Gunčar

    (Faculty of Chemistry and Chemical Technology, University of Ljubljana)

  • Kristina Djinović-Carugo

    (Faculty of Chemistry and Chemical Technology, University of Ljubljana
    Max F. Perutz Laboratories, University of Vienna)

  • Brigita Lenarčič

    (Faculty of Chemistry and Chemical Technology, University of Ljubljana
    Molecular and Structural Biology, Institute Jožef Stefan)

Abstract

EpCAM (epithelial cell adhesion molecule), a stem and carcinoma cell marker, is a cell surface protein involved in homotypic cell–cell adhesion via intercellular oligomerization and proliferative signalling via proteolytic cleavage. Despite its use as a diagnostic marker and being a drug target, structural details of this conserved vertebrate-exclusive protein remain unknown. Here we present the crystal structure of a heart-shaped dimer of the extracellular part of human EpCAM. The structure represents a cis-dimer that would form at cell surfaces and may provide the necessary structural foundation for the proposed EpCAM intercellular trans-tetramerization mediated by a membrane-distal region. By combining biochemical, biological and structural data on EpCAM, we show how proteolytic processing at various sites could influence structural integrity, oligomeric state and associated functionality of the molecule. We also describe the epitopes of this therapeutically important protein and explain the antigenicity of its regions.

Suggested Citation

  • Miha Pavšič & Gregor Gunčar & Kristina Djinović-Carugo & Brigita Lenarčič, 2014. "Crystal structure and its bearing towards an understanding of key biological functions of EpCAM," Nature Communications, Nature, vol. 5(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms5764
    DOI: 10.1038/ncomms5764
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    Cited by:

    1. Sumit J. Bandekar & Krassimira Garbett & Szymon P. Kordon & Ethan E. Dintzner & Jingxian Li & Tanner Shearer & Richard C. Sando & Demet Araç, 2025. "Structural basis for regulation of CELSR1 by a compact module in its extracellular region," Nature Communications, Nature, vol. 16(1), pages 1-15, December.

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