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Title | Cryo-EM structures of two human B cell receptor isotypes. |
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Journal, issue, pages | Science, Vol. 377, Issue 6608, Page 880-885, Year 2022 |
Publish date | Aug 19, 2022 |
![]() | Xinyu Ma / Yuwei Zhu / De Dong / Yan Chen / Shubo Wang / Dehui Yang / Zhuo Ma / Anqi Zhang / Fan Zhang / Changyou Guo / Zhiwei Huang / ![]() |
PubMed Abstract | The B cell receptor (BCR) complex plays a critical role in B cell development and immune responses. The assembly mechanisms underlying the BCR complex remain unknown. We determined the cryo-electron ...The B cell receptor (BCR) complex plays a critical role in B cell development and immune responses. The assembly mechanisms underlying the BCR complex remain unknown. We determined the cryo-electron microscopy (cryo-EM) structures of human IgG-BCR and IgM-BCR, which consist of membrane-bound immunoglobulin molecules (mIg) and Igα/β subunits at a 1:1 stoichiometry. Assembly of both BCR complexes involves their extracellular domains, membrane-proximal connection peptides, and transmembrane (TM) helices. The TM helices of mIgG and mIgM share a conserved set of hydrophobic and polar interactions with Igα/β TM helices. By contrast, the IgG-Cγ3 and IgM-Cμ4 domains interact with extracellular Ig-like domains of Igα/β through head-to-tail and side-by-side modes, respectively. This work reveals the structural basis for BCR assembly and provides insights into BCR triggering. |
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Methods | EM (single particle) |
Resolution | 3.03 - 3.63 Å |
Structure data | EMDB-32762, PDB-7wso: EMDB-33440, PDB-7xt6: |
Chemicals | ![]() ChemComp-NAG: |
Source |
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