Structural studies of the human α₁ glycine receptor via site-specific chemical cross-linking coupled with mass spectrometry.

ABSTRACT: By identifying distance constraints, chemical cross-linking coupled with mass spectrometry (CX-MS) can be a powerful complementary technique to other structural methods by interrogating macromolecular protein complexes under native-like conditions. In this study, we developed a CX-MS approach to identify the sites of chemical cross-linking from a single targeted location within the human α1 glycine receptor (α1 GlyR) in its apo state. The human α1 GlyR belongs to the family of pentameric ligand-gated ion channel receptors that function in fast neurotransmission. A single chemically reactive cysteine was reintroduced into a Cys null α1 GlyR construct at position 41 within the extracellular domain of human α1 homomeric GlyR overexpressed in a baculoviral system. After purification and recons

SUBMITTER: Veeramachaneni RJ 

PROVIDER: S-EPMC11550363 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature