Structural evolution of polymorphic class I HLA alleles, designating HLA-C with uncertain assemblies.

ABSTRACT: Hyper polymorphic major histocompatibility class I (MHC) molecules are key components for acquired immune responses. They have high specificity towards peptides presented to CD8 + T cells, resembling vaccine design and autoimmunity. However, a broader landscape over such a diverse set of evolutionary HLA molecules (in humans) and its structural variance in their crucial ectodomains or transmembrane regions remains elusive. Herein, we examined family-wide conserved HLA-A, HLA-B, and HLA-C alleles, and imputed structures over their full-length sequences. Despite high polymorphism among individual HLA molecules, the preserved amino acids remain proximal to C-terminus antigen binding sites. The HLA-A alleles with fewer evolutionary sub-branch have high affinity structures at both active (prese

SUBMITTER: Padariya M 

PROVIDER: S-EPMC12769140 | biostudies-literature | 2026

REPOSITORIES: biostudies-literature