| http://purl.uniprot.org/citations/22563102 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/22563102 | http://www.w3.org/2000/01/rdf-schema#comment | "The vertebrate calmodulin is configured with two structurally independent globular lobes in N- and C-terminus, and a flexible central linker. Distinctly, two lobes of calmodulin from Saccharomyces cerevisiae (yCaM) interact and influence the Ca(2+)-binding profile of each other. We explored this further using the mutant proteins with eliminated Ca(2+)-binding ability in one of the lobes and found that the Ca(2+)-bound N-lobe associates with the Ca(2+)-free C-lobe to gain the Ca(2+) affinity of a wild-type level. Next, analysing series of C-terminal residue truncation mutant, we found that the truncation of C-terminal three residues induce the hyper Ca(2+) affinity. These residues are also important for the general structural behaviour of calmodulin, such as Ca(2+)-induced slow mobility shift in polyacrylamide gel electrophoresis and for the ability to activate Cmk1p (yeast calmodulin kinase). These suggest: (i) when Ca(2+) occupies only N-lobe, two lobes interact and form the stable intermediate leading to a proper level of Ca(2+) affinity; (ii) the C-terminal three residues are required to prohibit abnormal stabilization of the intermediate promoting abnormally high Ca(2+) affinity and for recognition of target enzymes. A model for Ca(2+) and target bindings of yCaM is proposed. Evolutional aspect concerning the biological significance of this model was discussed."xsd:string |
| http://purl.uniprot.org/citations/22563102 | http://purl.org/dc/terms/identifier | "doi:10.1093/jb/mvs048"xsd:string |
| http://purl.uniprot.org/citations/22563102 | http://purl.uniprot.org/core/author | "Ishida H."xsd:string |
| http://purl.uniprot.org/citations/22563102 | http://purl.uniprot.org/core/author | "Nakashima K."xsd:string |
| http://purl.uniprot.org/citations/22563102 | http://purl.uniprot.org/core/author | "Yazawa M."xsd:string |
| http://purl.uniprot.org/citations/22563102 | http://purl.uniprot.org/core/author | "Nakatomi A."xsd:string |
| http://purl.uniprot.org/citations/22563102 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
| http://purl.uniprot.org/citations/22563102 | http://purl.uniprot.org/core/name | "J Biochem"xsd:string |
| http://purl.uniprot.org/citations/22563102 | http://purl.uniprot.org/core/pages | "27-35"xsd:string |
| http://purl.uniprot.org/citations/22563102 | http://purl.uniprot.org/core/title | "Specific conformation and Ca(2+)-binding mode of yeast calmodulin: insight into evolutionary development."xsd:string |
| http://purl.uniprot.org/citations/22563102 | http://purl.uniprot.org/core/volume | "152"xsd:string |
| http://purl.uniprot.org/citations/22563102 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/22563102 |
| http://purl.uniprot.org/citations/22563102 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/22563102 |
| http://purl.uniprot.org/uniprot/#_P27466-mappedCitation-22563102 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/22563102 |
| http://purl.uniprot.org/uniprot/#_P06787-mappedCitation-22563102 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/22563102 |
| http://purl.uniprot.org/uniprot/P06787 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/22563102 |
| http://purl.uniprot.org/uniprot/P27466 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/22563102 |