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TitleCryo-EM structure of the B cell co-receptor CD19 bound to the tetraspanin CD81.
Journal, issue, pagesScience, Vol. 371, Issue 6526, Page 300-305, Year 2021
Publish dateJan 15, 2021
AuthorsKatherine J Susa / Shaun Rawson / Andrew C Kruse / Stephen C Blacklow /
PubMed AbstractSignaling through the CD19-CD81 co-receptor complex, in combination with the B cell receptor, is a critical determinant of B cell development and activation. It is unknown how CD81 engages CD19 to ...Signaling through the CD19-CD81 co-receptor complex, in combination with the B cell receptor, is a critical determinant of B cell development and activation. It is unknown how CD81 engages CD19 to enable co-receptor function. Here, we report a 3.8-angstrom structure of the CD19-CD81 complex bound to a therapeutic antigen-binding fragment, determined by cryo-electron microscopy (cryo-EM). The structure includes both the extracellular domains and the transmembrane helices of the complex, revealing a contact interface between the ectodomains that drives complex formation. Upon binding to CD19, CD81 opens its ectodomain to expose a hydrophobic CD19-binding surface and reorganizes its transmembrane helices to occlude a cholesterol binding pocket present in the apoprotein. Our data reveal the structural basis for CD19-CD81 complex assembly, providing a foundation for rational design of therapies for B cell dysfunction.
External linksScience / PubMed:33446559
MethodsEM (single particle)
Resolution3.8 Å
Structure data

EMDB-22344, PDB-7jic:
Structure of human CD19-CD81 co-receptor complex bound to coltuximab Fab fragment
Method: EM (single particle) / Resolution: 3.8 Å

Source
  • homo sapiens (human)
  • mus musculus (house mouse)
KeywordsAmino Acid Sequence / Antibodies, Monoclonal, Humanized / Antigens, CD19 / B-Lymphocytes / Cryoelectron Microscopy / Humans / Maytansine / Models, Molecular / Mutation / Protein Binding / Protein Domains / Receptors, Antigen, B-Cell / Tetraspanin 28 / coltuximab ravtansine / IMMUNE SYSTEM / tetraspanin / Fab / complex

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