Alpha-conotoxin GeXXA

UniProtKB accession:  A0A0A0VBX4

Grouped By:  Matching UniProtKB accession

UniProtKB description:  Alpha-D-conopeptides act as non-competitive inhibitors of nicotinic acetylcholine receptors (nAChR). Through its two C-terminal domains, this homodimeric protein would bind to two nAChR allosteric sites, located outside the nAChR C-loop of the principal binding face and at the adjacent binding interface in a clockwise direction (By similarity). This toxin has strong inhibitory activity on rat alpha-9-alpha-10 (CHRNA9-CHRNA10) (IC(50)=1.2 nM) and a moderate inhibitory activity on human alpha-7 (CHRNA7) (IC(50)=210 nM), rat alpha-3-beta-2 (CHRNA3-CHRNB2) (IC(50)=498 nM), rat alpha-3-beta-4 (CHRNA3-CHRNB4) (IC(50)=614 nM) and rat alpha-1-beta-1-delta-epsilon (CHRNA1-CHRNB1-CHRNE-CHRND) (IC(50)=743 nM) subtypes (PubMed:26395518). Shows a weaker inhibitory activity on human alpha-9-alpha-10 (IC(50)=28 nM) than on the rat channel (PubMed:26395518). This is explained by a different residue in the probable binding site (His-31 in rat alpha-10 and Leu-31 in human) (PubMed:26395518).