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TitleStructural insights into the high-affinity IgE receptor FcεRI complex.
Journal, issue, pagesNature, Vol. 633, Issue 8031, Page 952-959, Year 2024
Publish dateAug 21, 2024
AuthorsMeijie Deng / Shuo Du / Handi Hou / Junyu Xiao /
PubMed AbstractImmunoglobulin E (IgE) plays a pivotal role in allergic responses. The high-affinity IgE receptor, FcεRI, found on mast cells and basophils, is central to the effector functions of IgE. FcεRI is a ...Immunoglobulin E (IgE) plays a pivotal role in allergic responses. The high-affinity IgE receptor, FcεRI, found on mast cells and basophils, is central to the effector functions of IgE. FcεRI is a tetrameric complex, comprising FcεRIα, FcεRIβ and a homodimer of FcRγ (originally known as FcεRIγ), with FcεRIα recognizing the Fc region of IgE (Fcε) and FcεRIβ-FcRγ facilitating signal transduction. Additionally, FcRγ is a crucial component of other immunoglobulin receptors, including those for IgG (FcγRI and FcγRIIIA) and IgA (FcαRI). However, the molecular basis of FcεRI assembly and the structure of FcRγ have remained elusive. Here we elucidate the cryogenic electron microscopy structure of the Fcε-FcεRI complex. FcεRIα has an essential role in the receptor's assembly, interacting with FcεRIβ and both FcRγ subunits. FcεRIβ is structured as a compact four-helix bundle, similar to the B cell antigen CD20. The FcRγ dimer exhibits an asymmetric architecture, and coils with the transmembrane region of FcεRIα to form a three-helix bundle. A cholesterol-like molecule enhances the interaction between FcεRIβ and the FcεRIα-FcRγ complex. Our mutagenesis analyses further indicate similarities between the interaction of FcRγ with FcεRIα and FcγRIIIA, but differences in that with FcαRI. These findings deepen our understanding of the signalling mechanisms of FcεRI and offer insights into the functionality of other immune receptors dependent on FcRγ.
External linksNature / PubMed:39169187
MethodsEM (single particle)
Resolution2.89 - 3.58 Å
Structure data

39029

8y81

EMDB-39029, PDB-8y81:
Structure of the ige-fc bound to its high affinity receptor fc(epsilon)ri
Method: EM (single particle) / Resolution: 2.89 Å

39032

8y84

EMDB-39032, PDB-8y84:
Structure of the high affinity receptor fc(epsilon)ri TM
Method: EM (single particle) / Resolution: 2.98 Å

39033

8z0t

EMDB-39033, PDB-8z0t:
Structure of the human ige-fc bound to its high affinity receptor fc(epsilon)
Method: EM (single particle) / Resolution: 3.58 Å

60089

8zgs

EMDB-60089, PDB-8zgs:
Structure of the ige-fc bound to its high affinity receptor fc(epsilon)ri state2
Method: EM (single particle) / Resolution: 3.04 Å

60090

8zgt

EMDB-60090, PDB-8zgt:
Structure of the ige-fc bound to its high affinity receptor fc(epsilon)ri state3
Method: EM (single particle) / Resolution: 2.96 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

Source
  • rattus norvegicus (Norway rat)
  • homo sapiens (human)
KeywordsIMMUNE SYSTEM / complex / antibody / ANTIBDOY / ANTIMICROBIAL PROTEIN / MEMBRANE PROTEIN

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