Elucidation of the molecular interactions that enable stable assembly and structural diversity in multicomponent immune receptors.

ABSTRACT: Multicomponent immune receptors are essential complexes in which distinct ligand-recognition and signaling subunits are held together by interactions between acidic and basic residues of their transmembrane helices. A 2:1 acidic-to-basic motif in the transmembrane domains of the subunits is necessary and sufficient to assemble these receptor complexes. Here, we study a prototype for these receptors, a DAP12-NKG2C 2:1 heterotrimeric complex, in which the two DAP12 subunits each contribute a single transmembrane Asp residue, and the NKG2C subunit contributes a Lys to form the complex. DAP12 can also associate with 20 other subunits using a similar motif. Here, we use molecular-dynamics simulations to understand the basis for the high affinity and diversity of interactions in this group of re

SUBMITTER: Fong LK 

PROVIDER: S-EPMC8256006 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature