The Intracellular Loop of the Glycine Receptor: It's not all about the Size.

摘要: The family of Cys-loop receptors (CLRs) shares a high degree homology and sequence identity. overall structural elements are highly conserved with large extracellular domain (ECD) harboring an α-helix 10 β-sheets. Following the ECD, four transmembrane domains (TMD) connected by intracellular loop structures. Except TM3-4 loop, their length comprises 7-14 residues. forms largest part (ICD) exhibits most variable region between all CLRs. ICD is defined together TM1-2 preceding ion channel pore. During last decade, crystallization approaches were successful for some members CLR family. To allow crystallization, was in structures replaced short linker present prokaryotic Therefore, no information about CLRs including glycine (GlyRs) available except basic stretches close to TM3 TM4. has been intensively studied regard functional aspects desensitization, modulation physiology pharmacological substances, posttranslational modifications, motifs important trafficking. Furthermore, interacts scaffold proteins enabling inhibitory synapse formation. This review focuses on attempts define within GlyRs discussed background protein-protein interactions formation absence loop.