PMID: 26416729

 

    Legend: Gene, Sites

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

Abstract :

1. Neurotransmitter-gated ion channels of the Cys-loop receptor family are essential mediators of fast neurotransmission throughout the nervous system and are implicated in many neurological disorders
2. Available X-ray structures of prokaryotic and eukaryotic Cys-loop receptors provide tremendous insights into the binding of agonists, the subsequent opening of the ion channel , and the mechanism of channel activation
3. Yet the mechanism of inactivation by antagonists remains unknown
4. Here we present a 3.0 Å X-ray structure of the human glycine receptor-α3 homopentamer in complex with a high affinity, high-specificity antagonist, strychnine
5. Our structure allows us to explore in detail the molecular recognition of antagonists
6. Comparisons with previous structures reveal a mechanism for antagonist-induced inactivation of Cys-loop receptors , involving an expansion of the orthosteric binding site in the extracellular domain that is coupled to closure of the ion pore in the transmembrane domain

Output (sent_index, trigger, protein, sugar, site):

Output(Part-Of) (sent_index, protein, site):

*Output_Site_Fusion* (sent_index, protein, sugar, site):

 

Protein	NCBI ID	SENTENCE INDEX