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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1997-7-1
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pubmed:abstractText |
beta2-Glycoprotein I was shown to bind reversibly to calmodulin in a Ca2+-dependent manner with a 1:1 stoichiometry, a Kd of 3 x 10(-9) M and a Hill coefficient of 1.4. A sequence in beta2-glycoprotein I (Lys-Pro-Gly-Tyr-Val-Ser-Arg-Gly-Gly-Met-Arg-Lys-Phe-Ile-) limited by Cys-32 and Cys-47 is suggested to be the calmodulin-binding region. This sequence was the only one in beta2-glycoprotein I theoretically having the ability to form a basic amphiphilic alpha-helix typical of a calmodulin binding sequence. The peptide corresponding to this sequence was synthesized and found to inhibit the interaction between beta2-glycoprotein I and calmodulin with an IC50 value of 0.38 x [beta2-glycoprotein I] and to displace the beta2-glycoprotein I from the beta2-glycoprotein I/calmodulin complex with an IC50 value of 0.90 x [beta2-glycoprotein I].
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
1339
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
217-25
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9187241-Animals,
pubmed-meshheading:9187241-Binding Sites,
pubmed-meshheading:9187241-Calmodulin,
pubmed-meshheading:9187241-Cattle,
pubmed-meshheading:9187241-Glycoproteins,
pubmed-meshheading:9187241-Humans,
pubmed-meshheading:9187241-Phosphorylation,
pubmed-meshheading:9187241-Radioimmunoassay,
pubmed-meshheading:9187241-Spectrometry, Fluorescence,
pubmed-meshheading:9187241-Tryptophan,
pubmed-meshheading:9187241-beta 2-Glycoprotein I
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pubmed:year |
1997
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pubmed:articleTitle |
Characterization of the interaction between beta2-glycoprotein I and calmodulin, and identification of a binding sequence in beta2-glycoprotein I.
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pubmed:affiliation |
Department of Medical Biochemistry and Genetics, The Panum Institute, University of Copenhagen, Copenhagen N, Denmark.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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