| http://purl.uniprot.org/citations/11055992 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11055992 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11055992 | http://www.w3.org/2000/01/rdf-schema#comment | "The gating modifier toxins are a large family of protein toxins that modify either activation or inactivation of voltage-gated ion channels. omega-Aga-IVA is a gating modifier toxin from spider venom that inhibits voltage-gated Ca(2+) channels by shifting activation to more depolarized voltages. We identified two Glu residues near the COOH-terminal edge of S3 in the alpha(1A) Ca(2+) channel (one in repeat I and the other in repeat IV) that align with Glu residues previously implicated in forming the binding sites for gating modifier toxins on K(+) and Na(+) channels. We found that mutation of the Glu residue in repeat I of the Ca(2+) channel had no significant effect on inhibition by omega-Aga-IVA, whereas the equivalent mutation of the Glu in repeat IV disrupted inhibition by the toxin. These results suggest that the COOH-terminal end of S3 within repeat IV contributes to forming a receptor for omega-Aga-IVA. The strong predictive value of previous mapping studies for K(+) and Na(+) channel toxins argues for a conserved binding motif for gating modifier toxins within the voltage-sensing domains of voltage-gated ion channels."xsd:string |
| http://purl.uniprot.org/citations/11055992 | http://purl.org/dc/terms/identifier | "doi:10.1085/jgp.116.5.637"xsd:string |
| http://purl.uniprot.org/citations/11055992 | http://purl.org/dc/terms/identifier | "doi:10.1085/jgp.116.5.637"xsd:string |
| http://purl.uniprot.org/citations/11055992 | http://purl.uniprot.org/core/author | "Swartz K.J."xsd:string |
| http://purl.uniprot.org/citations/11055992 | http://purl.uniprot.org/core/author | "Swartz K.J."xsd:string |
| http://purl.uniprot.org/citations/11055992 | http://purl.uniprot.org/core/author | "Winterfield J.R."xsd:string |
| http://purl.uniprot.org/citations/11055992 | http://purl.uniprot.org/core/author | "Winterfield J.R."xsd:string |
| http://purl.uniprot.org/citations/11055992 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
| http://purl.uniprot.org/citations/11055992 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
| http://purl.uniprot.org/citations/11055992 | http://purl.uniprot.org/core/name | "J. Gen. Physiol."xsd:string |
| http://purl.uniprot.org/citations/11055992 | http://purl.uniprot.org/core/name | "J. Gen. Physiol."xsd:string |
| http://purl.uniprot.org/citations/11055992 | http://purl.uniprot.org/core/pages | "637-644"xsd:string |
| http://purl.uniprot.org/citations/11055992 | http://purl.uniprot.org/core/pages | "637-644"xsd:string |
| http://purl.uniprot.org/citations/11055992 | http://purl.uniprot.org/core/title | "A hot spot for the interaction of gating modifier toxins with voltage-dependent ion channels."xsd:string |
| http://purl.uniprot.org/citations/11055992 | http://purl.uniprot.org/core/title | "A hot spot for the interaction of gating modifier toxins with voltage-dependent ion channels."xsd:string |
| http://purl.uniprot.org/citations/11055992 | http://purl.uniprot.org/core/volume | "116"xsd:string |
| http://purl.uniprot.org/citations/11055992 | http://purl.uniprot.org/core/volume | "116"xsd:string |
| http://purl.uniprot.org/citations/11055992 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11055992 |
| http://purl.uniprot.org/citations/11055992 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11055992 |
| http://purl.uniprot.org/citations/11055992 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/11055992 |
| http://purl.uniprot.org/citations/11055992 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/11055992 |
| http://purl.uniprot.org/uniprot/P30288 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/11055992 |
| http://purl.uniprot.org/uniprot/P27884 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/11055992 |