Extended Data Figure 5 : Sequence alignment of GlyRα3cryst with representative eukaryotic Cys-loop receptor family members.

From: Crystal structure of human glycine receptor-α3 bound to antagonist strychnine

Extended Data Figure 5

Residue conservation is indicated by grey and black highlights. Site of N-linked glycosylation of GlyRα3cryst is indicated by the orange hexagon. Residues involved in binding of strychnine are indicated by green (the principal subunit) and cyan (the complementary subunit) dots. Red triangles above residues indicate mutations in GlyRα1 or GlyRβ that cause hyperekplexia. Signal peptides have been removed from all protein sequences. Secondary structure elements are denoted by cylinders (helices) and arrows (strands) above the alignment. The alignment was generated using ClustalW. Protein sequences are from the following entires: human GlyRα1 (Uniprot P23415), human GlyRβ (Uniprot 48167), GluClcryst (PDB accession number 4TNV), GABAAR-β3cryst (PDB accession number 4COF), and 5HT3A (PDB accession number 4PIR).