| http://purl.uniprot.org/citations/27876793 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/27876793 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/27876793 | http://www.w3.org/2000/01/rdf-schema#comment | "PEP-19 is a small protein that increases the rates of Ca2+ binding to the C-domain of calmodulin (CaM) by an unknown mechanism. Although an IQ motif promotes binding to CaM, an acidic sequence in PEP-19 is required to modulate Ca2+ binding and to sensitize HeLa cells to ATP-induced Ca2+ release. Here, we report the NMR solution structure of a complex between PEP-19 and the C-domain of apo CaM. The acidic sequence of PEP-19 associates between helices E and F of CaM via hydrophobic interactions. This allows the acidic side chains in PEP-19 to extend toward the solvent and form a negatively charged surface that resembles a catcher's mitt near Ca2+ binding loop III of CaM. The topology and gradients of negative electrostatic surface potential support a mechanism by which PEP-19 increases the rate of Ca2+ binding to the C-domain of CaM by 'catching' and electrostatically steering Ca2+ to site III."xsd:string |
| http://purl.uniprot.org/citations/27876793 | http://purl.org/dc/terms/identifier | "doi:10.1038/ncomms13583"xsd:string |
| http://purl.uniprot.org/citations/27876793 | http://purl.org/dc/terms/identifier | "doi:10.1038/ncomms13583"xsd:string |
| http://purl.uniprot.org/citations/27876793 | http://purl.uniprot.org/core/author | "Wang X."xsd:string |
| http://purl.uniprot.org/citations/27876793 | http://purl.uniprot.org/core/author | "Wang X."xsd:string |
| http://purl.uniprot.org/citations/27876793 | http://purl.uniprot.org/core/author | "Putkey J.A."xsd:string |
| http://purl.uniprot.org/citations/27876793 | http://purl.uniprot.org/core/author | "Putkey J.A."xsd:string |
| http://purl.uniprot.org/citations/27876793 | http://purl.uniprot.org/core/date | "2016"xsd:gYear |
| http://purl.uniprot.org/citations/27876793 | http://purl.uniprot.org/core/date | "2016"xsd:gYear |
| http://purl.uniprot.org/citations/27876793 | http://purl.uniprot.org/core/name | "Nat. Commun."xsd:string |
| http://purl.uniprot.org/citations/27876793 | http://purl.uniprot.org/core/name | "Nat. Commun."xsd:string |
| http://purl.uniprot.org/citations/27876793 | http://purl.uniprot.org/core/pages | "13583"xsd:string |
| http://purl.uniprot.org/citations/27876793 | http://purl.uniprot.org/core/pages | "13583"xsd:string |
| http://purl.uniprot.org/citations/27876793 | http://purl.uniprot.org/core/title | "PEP-19 modulates calcium binding to calmodulin by electrostatic steering."xsd:string |
| http://purl.uniprot.org/citations/27876793 | http://purl.uniprot.org/core/title | "PEP-19 modulates calcium binding to calmodulin by electrostatic steering."xsd:string |
| http://purl.uniprot.org/citations/27876793 | http://purl.uniprot.org/core/volume | "7"xsd:string |
| http://purl.uniprot.org/citations/27876793 | http://purl.uniprot.org/core/volume | "7"xsd:string |
| http://purl.uniprot.org/citations/27876793 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/27876793 |
| http://purl.uniprot.org/citations/27876793 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/27876793 |
| http://purl.uniprot.org/citations/27876793 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/27876793 |
| http://purl.uniprot.org/citations/27876793 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/27876793 |
| http://purl.uniprot.org/uniprot/P48539 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/27876793 |
| http://purl.uniprot.org/uniprot/P0DP23 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/27876793 |