pubmed-article:9100027 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9100027 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
pubmed-article:9100027 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
pubmed-article:9100027 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
pubmed-article:9100027 | lifeskim:mentions | umls-concept:C0006772 | lld:lifeskim |
pubmed-article:9100027 | lifeskim:mentions | umls-concept:C0005456 | lld:lifeskim |
pubmed-article:9100027 | lifeskim:mentions | umls-concept:C2346927 | lld:lifeskim |
pubmed-article:9100027 | lifeskim:mentions | umls-concept:C1521840 | lld:lifeskim |
pubmed-article:9100027 | pubmed:issue | 14 | lld:pubmed |
pubmed-article:9100027 | pubmed:dateCreated | 1997-5-15 | lld:pubmed |
pubmed-article:9100027 | pubmed:abstractText | The binding of Mg2+ to calmodulin (CaM) and the effect of Mg2+ on the binding of Ca2+-CaM to target peptides were examined using two-dimensional nuclear magnetic resonance and fluorescence spectroscopic techniques. We found that Mg2+ preferentially binds to Ca2+-binding sites I and IV of CaM in the absence of Ca2+ and that Ca2+-binding site III displays the lowest affinity for Mg2+. In contrast to the marked structural transitions induced by Ca2+ binding, Mg2+ binding causes only localized conformational changes within the four Ca2+-binding loops of CaM. Therefore, Mg2+ does not seem to be able to cause significant structural effects required for the interaction of CaM with target proteins. The presence of excess Mg2+ (up to 10 mM) does not change the order and cooperativity of Ca2+ binding to CaM, and as expected, the structure of Ca2+-saturated CaM is not affected by the presence of Mg2+. However, we found that the binding of Ca2+-saturated CaM to target peptides is affected by Mg2+ with the binding affinity decreasing as the Mg2+ concentration increases. Three different peptides, corresponding to the CaM binding domain of skeletal muscle myosin light-chain kinase (MLCK), CaM-dependent cyclic nucleotide phosphodiesterase (PDE), and smooth muscle caldesmon (CaD), were examined and show different reductions in their affinities toward CaM. The CaM-binding affinity of the MLCK peptide in the presence of 50 mM Mg2+ is approximately 40-fold lower than that seen in the absence of Mg2+, and a similar response was observed for the PDE peptide. The affinity of the CaD peptide for CaM also shows a Mg2+ dependence, though to a much lower magnitude. The Mg2+-dependent decrease in the affinities between CaM and its target peptides is an intrinsic property of Mg2+ rather than a nonspecific ionic effect, as other metal ions such as Na+ do not completely replicate the effect of Mg2+. The inhibitory effect of Mg2+ on the formation of complexes between CaM and its targets may contribute to the specificity of CaM in target activation in response to cellular Ca2+ concentration fluctuations. | lld:pubmed |
pubmed-article:9100027 | pubmed:language | eng | lld:pubmed |
pubmed-article:9100027 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9100027 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:9100027 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9100027 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9100027 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9100027 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9100027 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9100027 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9100027 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9100027 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9100027 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9100027 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9100027 | pubmed:month | Apr | lld:pubmed |
pubmed-article:9100027 | pubmed:issn | 0006-2960 | lld:pubmed |
pubmed-article:9100027 | pubmed:author | pubmed-author:OhkiSS | lld:pubmed |
pubmed-article:9100027 | pubmed:author | pubmed-author:ZhangMM | lld:pubmed |
pubmed-article:9100027 | pubmed:author | pubmed-author:IkuraMM | lld:pubmed |
pubmed-article:9100027 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9100027 | pubmed:day | 8 | lld:pubmed |
pubmed-article:9100027 | pubmed:volume | 36 | lld:pubmed |
pubmed-article:9100027 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9100027 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9100027 | pubmed:pagination | 4309-16 | lld:pubmed |
pubmed-article:9100027 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
pubmed-article:9100027 | pubmed:meshHeading | pubmed-meshheading:9100027-... | lld:pubmed |
pubmed-article:9100027 | pubmed:meshHeading | pubmed-meshheading:9100027-... | lld:pubmed |
pubmed-article:9100027 | pubmed:meshHeading | pubmed-meshheading:9100027-... | lld:pubmed |
pubmed-article:9100027 | pubmed:meshHeading | pubmed-meshheading:9100027-... | lld:pubmed |
pubmed-article:9100027 | pubmed:meshHeading | pubmed-meshheading:9100027-... | lld:pubmed |
pubmed-article:9100027 | pubmed:meshHeading | pubmed-meshheading:9100027-... | lld:pubmed |
pubmed-article:9100027 | pubmed:meshHeading | pubmed-meshheading:9100027-... | lld:pubmed |
pubmed-article:9100027 | pubmed:meshHeading | pubmed-meshheading:9100027-... | lld:pubmed |
pubmed-article:9100027 | pubmed:meshHeading | pubmed-meshheading:9100027-... | lld:pubmed |
pubmed-article:9100027 | pubmed:meshHeading | pubmed-meshheading:9100027-... | lld:pubmed |
pubmed-article:9100027 | pubmed:meshHeading | pubmed-meshheading:9100027-... | lld:pubmed |
pubmed-article:9100027 | pubmed:meshHeading | pubmed-meshheading:9100027-... | lld:pubmed |
pubmed-article:9100027 | pubmed:meshHeading | pubmed-meshheading:9100027-... | lld:pubmed |
pubmed-article:9100027 | pubmed:meshHeading | pubmed-meshheading:9100027-... | lld:pubmed |
pubmed-article:9100027 | pubmed:meshHeading | pubmed-meshheading:9100027-... | lld:pubmed |
pubmed-article:9100027 | pubmed:meshHeading | pubmed-meshheading:9100027-... | lld:pubmed |
pubmed-article:9100027 | pubmed:year | 1997 | lld:pubmed |
pubmed-article:9100027 | pubmed:articleTitle | Identification of Mg2+-binding sites and the role of Mg2+ on target recognition by calmodulin. | lld:pubmed |
pubmed-article:9100027 | pubmed:affiliation | Department of Biochemistry, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon. | lld:pubmed |
pubmed-article:9100027 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9100027 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9100027 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9100027 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9100027 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9100027 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9100027 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9100027 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9100027 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9100027 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9100027 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9100027 | lld:pubmed |