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| Title | Cryo-EM structure of the B cell co-receptor CD19 bound to the tetraspanin CD81. |
|---|---|
| Journal, issue, pages | Science, Vol. 371, Issue 6526, Page 300-305, Year 2021 |
| Publish date | Jan 15, 2021 |
 Authors | Katherine J Susa / Shaun Rawson / Andrew C Kruse / Stephen C Blacklow /  |
| PubMed Abstract | 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 ...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 links | Science / PubMed:33446559 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 3.8 Å |
| Structure data | EMDB-22344, PDB-7jic: |
| Source |
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 Keywords | IMMUNE SYSTEM / tetraspanin / Fab / complex |
homo sapiens (human)
mus musculus (house mouse)
