Source:http://linkedlifedata.com/resource/pubmed/id/18853393
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
22
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pubmed:dateCreated |
2008-11-4
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pubmed:abstractText |
Amphibian peptides which inhibit the formation of nitric oxide by neuronal nitric oxide synthase (nNOS) do so by binding to the protein cofactor, Ca2+calmodulin (Ca2+CaM). Complex formation between active peptides and Ca2+CaM has been demonstrated by negative ion electrospray ionisation mass spectrometry using an aqueous ammonium acetate buffer system. In all cases studied, the assemblies are formed with a 1:1:4 calmodulin/peptide/Ca2+ stoichiometry. In contrast, the complex involving the 20-residue binding domain of the plasma Ca2+ pump C20W (LRRGQILWFRGLNRIQTQIK-OH) with CaM has been shown by previous two-dimensional nuclear magnetic resonance (2D NMR) studies to involve complexation of the C-terminal end of CaM. Under identical conditions to those used for the amphibian peptide study, the ESI complex between C20W and CaM shows specific 1:1:2 stoichiometry. Since complex formation with the studied amphibian peptides requires Ca2+CaM to contain its full complement of four Ca2+ ions, this indicates that the amphibian peptides require both ends of the CaM to effect complex formation. Charge-state analysis and an H/D exchange experiment (with caerin 1.8) suggest that complexation involves Ca2+CaM undergoing a conformational change to a more compact structure.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amphibian Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase Type I,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0951-4198
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
22
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3501-9
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pubmed:meshHeading |
pubmed-meshheading:18853393-Amphibian Proteins,
pubmed-meshheading:18853393-Animals,
pubmed-meshheading:18853393-Anura,
pubmed-meshheading:18853393-Binding Sites,
pubmed-meshheading:18853393-Calcium,
pubmed-meshheading:18853393-Calmodulin,
pubmed-meshheading:18853393-Nitric Oxide Synthase Type I,
pubmed-meshheading:18853393-Peptides,
pubmed-meshheading:18853393-Protein Binding,
pubmed-meshheading:18853393-Spectrometry, Mass, Electrospray Ionization
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pubmed:year |
2008
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pubmed:articleTitle |
Binding studies of nNOS-active amphibian peptides and Ca2+ calmodulin, using negative ion electrospray ionisation mass spectrometry.
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pubmed:affiliation |
Department of Chemistry, The University of Adelaide, South Australia, 5005, Australia.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Evaluation Studies
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