Table 1 Characteristics of seven identified HLA-G isoforms
From: Harnessing the potential of HLA-G in cancer therapy: advances, challenges, and prospects
Isoform | Type | Alternative splicing | Structure characteristics |
|---|---|---|---|
HLA-G1 | Membrane-bound | Full-length, wild type | Has α1, α2, and α3 domains, non-covalently bind to β2-microglobulin (β2m) |
HLA-G2 | Membrane-bound | Without exon 3 | Has α1 and α3 domains, lack of α2 domain, non-covalently bind to β2m |
HLA-G3 | Membrane-bound | Without exon 3 and exon 4 | The shortest isoform, only has α1 domain |
HLA-G4 | membrane-bound | Without exon 4 | Has α1 and α2 domains, lack of α3 domain |
HLA-G5 | Soluble | Contains intron 4 (with an early stop codon) | Without transmembrane domain, has α1, α2, and α3 domains, non-covalently bind to β2m |
HLA-G6 | Soluble | Contains intron 4 (with an early stop codon) | Without transmembrane domain, has α1 and α3 domains, non-covalently bind to β2m |
HLA-G7 | Soluble | Contains intron 2 (with an early stop codon) | Without transmembrane domain, only has α1 domain |