+Search query
-Structure paper
Title | Cryo-EM structure of the human IgM B cell receptor. |
---|---|
Journal, issue, pages | Science, Vol. 377, Issue 6608, Page 875-880, Year 2022 |
Publish date | Aug 19, 2022 |
Authors | Qiang Su / Mengying Chen / Yan Shi / Xiaofeng Zhang / Gaoxingyu Huang / Bangdong Huang / Dongwei Liu / Zhangsuo Liu / Yigong Shi / |
PubMed Abstract | The B cell receptor (BCR) initiates immune responses through antigen recognition. We report a 3.3-angstrom cryo-electron microscopy structure of human immunoglobulin M (IgM)-BCR in the resting state. ...The B cell receptor (BCR) initiates immune responses through antigen recognition. We report a 3.3-angstrom cryo-electron microscopy structure of human immunoglobulin M (IgM)-BCR in the resting state. IgM-BCR comprises two heavy chains, two light chains, and the Igα/Igβ heterodimer. The ectodomains of the heavy chains closely stack against those of Igα/Igβ, with one heavy chain locked between Igα and Igβ in the juxtamembrane region. Extracellular interactions may determine isotype specificity of the BCR. The transmembrane helices of IgM-BCR form a four-helix bundle that appears to be conserved among all BCR isotypes. This structure contains 14 glycosylation sites on the IgM-BCR ectodomains and reveals three potential surface binding sites. Our work reveals the organizational principles of the BCR and may facilitate the design of antibody-based therapeutics. |
External links | Science / PubMed:35981043 |
Methods | EM (single particle) |
Resolution | 3.3 Å |
Structure data | EMDB-33390, PDB-7xq8: |
Chemicals | ChemComp-NAG: |
Source |
|
Keywords | SIGNALING PROTEIN / immunology / B cell signalling / adaptive immunity / antibody |