Crosslinking constraints and computational models as complementary tools in modeling the extracellular domain of the glycine receptor.

ABSTRACT: The glycine receptor (GlyR), a member of the pentameric ligand-gated ion channel superfamily, is the major inhibitory neurotransmitter-gated receptor in the spinal cord and brainstem. In these receptors, the extracellular domain binds agonists, antagonists and various other modulatory ligands that act allosterically to modulate receptor function. The structures of homologous receptors and binding proteins provide templates for modeling of the ligand-binding domain of GlyR, but limitations in sequence homology and structure resolution impact on modeling studies. The determination of distance constraints via chemical crosslinking studies coupled with mass spectrometry can provide additional structural information to aid in model refinement, however it is critical to be able to distinguish be

SUBMITTER: Liu Z 

PROVIDER: S-EPMC4099341 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature