Cryo-EM structures of two human B cell receptor isotypes.
Science
; 377(6608): 880-885, 2022 08 19.
Article
em En
| MEDLINE
| ID: mdl-35981028
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 microscopy (cryo-EM) structures of human IgG-BCR and IgM-BCR, which consist of membrane-bound immunoglobulin molecules (mIg) and Igα/ß subunits at a 11 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/ß TM helices. By contrast, the IgG-Cγ3 and IgM-Cµ4 domains interact with extracellular Ig-like domains of Igα/ß 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.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Imunoglobulina G
/
Imunoglobulina M
/
Antígenos CD79
Limite:
Humans
Idioma:
En
Revista:
Science
Ano de publicação:
2022
Tipo de documento:
Article
País de afiliação:
China