| http://purl.uniprot.org/citations/23607618 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/23607618 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/23607618 | http://www.w3.org/2000/01/rdf-schema#comment | "Calmodulin (CaM) is a calcium binding protein that plays numerous roles in Ca-dependent cellular processes, including uptake and release of neurotransmitters in neurons. α-Synuclein (α-syn), one of the most abundant proteins in central nervous system neurons, helps maintain presynaptic vesicles containing neurotransmitters and moderates their Ca-dependent release into the synapse. Ca-Bound CaM interacts with α-syn most strongly at its N-terminus. The N-terminal region of α-syn is important for membrane binding; thus, CaM could modulate membrane association of α-syn in a Ca-dependent manner. In contrast, Ca-free CaM has negligible interaction. The interaction with CaM leads to significant signal broadening in both CaM and α-syn NMR spectra, most likely due to conformational exchange. The broadening is much reduced when binding a peptide consisting of the first 19 residues of α-syn. In neurons, most α-syn is acetylated at the N-terminus, and acetylation leads to a 10-fold increase in binding strength for the α-syn peptide (KD = 35 ± 10 μM). The N-terminally acetylated peptide adopts a helical structure at the N-terminus with the acetyl group contacting the N-terminal domain of CaM and with less ordered helical structure toward the C-terminus of the peptide contacting the CaM C-terminal domain. Comparison with known structures shows that the CaM/α-syn complex most closely resembles Ca-bound CaM in a complex with an IQ motif peptide. However, a search comparing the α-syn peptide sequence with known CaM targets, including IQ motifs, found no homologies; thus, the N-terminal α-syn CaM binding site appears to be a novel CaM target sequence."xsd:string |
| http://purl.uniprot.org/citations/23607618 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi400199p"xsd:string |
| http://purl.uniprot.org/citations/23607618 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi400199p"xsd:string |
| http://purl.uniprot.org/citations/23607618 | http://purl.uniprot.org/core/author | "Lee J.C."xsd:string |
| http://purl.uniprot.org/citations/23607618 | http://purl.uniprot.org/core/author | "Lee J.C."xsd:string |
| http://purl.uniprot.org/citations/23607618 | http://purl.uniprot.org/core/author | "Yap T.L."xsd:string |
| http://purl.uniprot.org/citations/23607618 | http://purl.uniprot.org/core/author | "Yap T.L."xsd:string |
| http://purl.uniprot.org/citations/23607618 | http://purl.uniprot.org/core/author | "Gruschus J.M."xsd:string |
| http://purl.uniprot.org/citations/23607618 | http://purl.uniprot.org/core/author | "Gruschus J.M."xsd:string |
| http://purl.uniprot.org/citations/23607618 | http://purl.uniprot.org/core/author | "Maltsev A.S."xsd:string |
| http://purl.uniprot.org/citations/23607618 | http://purl.uniprot.org/core/author | "Maltsev A.S."xsd:string |
| http://purl.uniprot.org/citations/23607618 | http://purl.uniprot.org/core/author | "Pistolesi S."xsd:string |
| http://purl.uniprot.org/citations/23607618 | http://purl.uniprot.org/core/author | "Pistolesi S."xsd:string |
| http://purl.uniprot.org/citations/23607618 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/23607618 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/23607618 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/23607618 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/23607618 | http://purl.uniprot.org/core/pages | "3436-3445"xsd:string |
| http://purl.uniprot.org/citations/23607618 | http://purl.uniprot.org/core/pages | "3436-3445"xsd:string |
| http://purl.uniprot.org/citations/23607618 | http://purl.uniprot.org/core/title | "NMR structure of calmodulin complexed to an N-terminally acetylated alpha-synuclein peptide."xsd:string |
| http://purl.uniprot.org/citations/23607618 | http://purl.uniprot.org/core/title | "NMR structure of calmodulin complexed to an N-terminally acetylated alpha-synuclein peptide."xsd:string |
| http://purl.uniprot.org/citations/23607618 | http://purl.uniprot.org/core/volume | "52"xsd:string |
| http://purl.uniprot.org/citations/23607618 | http://purl.uniprot.org/core/volume | "52"xsd:string |