| http://purl.uniprot.org/citations/27114612 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/27114612 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/27114612 | http://www.w3.org/2000/01/rdf-schema#comment | "Calcins are a novel family of scorpion peptides that bind with high affinity to ryanodine receptors (RyRs) and increase their activity by inducing subconductance states. Here, we provide a comprehensive analysis of the structure-function relationships of the eight calcins known to date, based on their primary sequence, three-dimensional modeling, and functional effects on skeletal RyRs (RyR1). Primary sequence alignment and evolutionary analysis show high similarity among all calcins (≥78.8% identity). Other common characteristics include an inhibitor cysteine knot (ICK) motif stabilized by three pairs of disulfide bridges and a dipole moment (DM) formed by positively charged residues clustering on one side of the molecule and neutral and negatively charged residues segregating on the opposite side. [(3)H]Ryanodine binding assays, used as an index of the open probability of RyRs, reveal that all eight calcins activate RyR1 dose-dependently with Kd values spanning approximately three orders of magnitude and in the following rank order: opicalcin1 > opicalcin2 > vejocalcin > hemicalcin > imperacalcin > hadrucalcin > maurocalcin >> urocalcin. All calcins significantly augment the bell-shaped [Ca(2+)]-[(3)H]ryanodine binding curve with variable effects on the affinity constants for Ca(2+) activation and inactivation. In single channel recordings, calcins induce the appearance of a subconductance state in RyR1 that has a unique fractional value (∼20% to ∼60% of the full conductance state) but bears no relationship to binding affinity, DM, or capacity to stimulate Ca(2+) release. Except for urocalcin, all calcins at 100 nM concentration stimulate Ca(2+) release and deplete Ca(2+) load from skeletal sarcoplasmic reticulum. The natural variation within the calcin family of peptides offers a diversified set of high-affinity ligands with the capacity to modulate RyRs with high dynamic range and potency."xsd:string |
| http://purl.uniprot.org/citations/27114612 | http://purl.org/dc/terms/identifier | "doi:10.1085/jgp.201511499"xsd:string |
| http://purl.uniprot.org/citations/27114612 | http://purl.org/dc/terms/identifier | "doi:10.1085/jgp.201511499"xsd:string |
| http://purl.uniprot.org/citations/27114612 | http://purl.uniprot.org/core/author | "Gurrola G.B."xsd:string |
| http://purl.uniprot.org/citations/27114612 | http://purl.uniprot.org/core/author | "Gurrola G.B."xsd:string |
| http://purl.uniprot.org/citations/27114612 | http://purl.uniprot.org/core/author | "Possani L.D."xsd:string |
| http://purl.uniprot.org/citations/27114612 | http://purl.uniprot.org/core/author | "Possani L.D."xsd:string |
| http://purl.uniprot.org/citations/27114612 | http://purl.uniprot.org/core/author | "Zhang J."xsd:string |
| http://purl.uniprot.org/citations/27114612 | http://purl.uniprot.org/core/author | "Zhang J."xsd:string |
| http://purl.uniprot.org/citations/27114612 | http://purl.uniprot.org/core/author | "Zhang L."xsd:string |
| http://purl.uniprot.org/citations/27114612 | http://purl.uniprot.org/core/author | "Zhang L."xsd:string |
| http://purl.uniprot.org/citations/27114612 | http://purl.uniprot.org/core/author | "Xiao L."xsd:string |
| http://purl.uniprot.org/citations/27114612 | http://purl.uniprot.org/core/author | "Xiao L."xsd:string |
| http://purl.uniprot.org/citations/27114612 | http://purl.uniprot.org/core/author | "Zamudio F.Z."xsd:string |
| http://purl.uniprot.org/citations/27114612 | http://purl.uniprot.org/core/author | "Zamudio F.Z."xsd:string |
| http://purl.uniprot.org/citations/27114612 | http://purl.uniprot.org/core/author | "SanMartin M."xsd:string |
| http://purl.uniprot.org/citations/27114612 | http://purl.uniprot.org/core/author | "SanMartin M."xsd:string |
| http://purl.uniprot.org/citations/27114612 | http://purl.uniprot.org/core/author | "Valdivia C.R."xsd:string |
| http://purl.uniprot.org/citations/27114612 | http://purl.uniprot.org/core/author | "Valdivia C.R."xsd:string |
| http://purl.uniprot.org/citations/27114612 | http://purl.uniprot.org/core/author | "Valdivia H.H."xsd:string |
| http://purl.uniprot.org/citations/27114612 | http://purl.uniprot.org/core/author | "Valdivia H.H."xsd:string |
| http://purl.uniprot.org/citations/27114612 | http://purl.uniprot.org/core/date | "2016"xsd:gYear |
| http://purl.uniprot.org/citations/27114612 | http://purl.uniprot.org/core/date | "2016"xsd:gYear |