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rdf:type |
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lifeskim:mentions |
umls-concept:C0005456,
umls-concept:C0054493,
umls-concept:C0205214,
umls-concept:C0218111,
umls-concept:C0237876,
umls-concept:C0521324,
umls-concept:C0913382,
umls-concept:C1514562,
umls-concept:C1711351,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
6
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pubmed:dateCreated |
2005-2-7
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pubmed:abstractText |
Maurocalcine is a scorpion venom toxin of 33 residues that bears a striking resemblance to the domain A of the dihydropyridine voltage-dependent calcium channel type 1.1 (Cav1.1) subunit. This domain belongs to the II-III loop of Cav1.1, which is implicated in excitation-contraction coupling. Besides the structural homology, maurocalcine also modulates RyR1 channel activity in a manner akin to a synthetic peptide of domain A. Because of these similarities, we hypothesized that maurocalcine and domain A may bind onto an identical region(s) of RyR1. Using a set of RyR1 fragments, we demonstrate that peptide A and maurocalcine bind onto two discrete RyR1 regions: fragments 3 and 7 encompassing residues 1021-1631 and 3201-3661, respectively. The binding onto fragment 7 is of greater importance and was thus further investigated. We found that the amino acid region 3351-3507 of RyR1 (fragment 7.2) is sufficient for these interactions. Proof that peptide A and maurocalcine bind onto the same site is provided by competition experiments in which binding of fragment 7.2 to peptide A is inhibited by preincubation with maurocalcine. Moreover, when expressed in COS-7 cells, RyR1 carrying a deletion of fragment 7 shows a loss of interaction with both peptide A and maurocalcine. At the functional level, this deletion abolishes the maurocalcine induced stimulation of [3H]ryanodine binding onto microsomes of transfected COS-7 cells without affecting the caffeine and ATP responses.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15591063-10075681,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15591063-10713267,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15591063-10861934,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15591063-11751303,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15591063-12045016,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15591063-12429019,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15591063-12496092,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15591063-1249731,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15591063-12586831,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15591063-12869557,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15591063-12900411,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15591063-14535845,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15591063-1654596,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15591063-2165570,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15591063-2448641,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15591063-7673188,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15591063-8134386,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15591063-8598910,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15591063-8751443,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15591063-9176137,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15591063-9358051,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15591063-9593671,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15591063-9737952,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15591063-9792715,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15591063-9895277
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium Channels, L-Type,
http://linkedlifedata.com/resource/pubmed/chemical/Caveolin 1,
http://linkedlifedata.com/resource/pubmed/chemical/Caveolins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ryanodine,
http://linkedlifedata.com/resource/pubmed/chemical/Ryanodine Receptor Calcium Release...,
http://linkedlifedata.com/resource/pubmed/chemical/Scorpion Venoms,
http://linkedlifedata.com/resource/pubmed/chemical/maurocalcine
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
280
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4013-6
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:15591063-Adenosine Triphosphate,
pubmed-meshheading:15591063-Animals,
pubmed-meshheading:15591063-Binding, Competitive,
pubmed-meshheading:15591063-Binding Sites,
pubmed-meshheading:15591063-COS Cells,
pubmed-meshheading:15591063-Calcium Channels, L-Type,
pubmed-meshheading:15591063-Caveolin 1,
pubmed-meshheading:15591063-Caveolins,
pubmed-meshheading:15591063-Chromatography,
pubmed-meshheading:15591063-Cloning, Molecular,
pubmed-meshheading:15591063-Cryoelectron Microscopy,
pubmed-meshheading:15591063-Microscopy, Fluorescence,
pubmed-meshheading:15591063-Muscle, Skeletal,
pubmed-meshheading:15591063-Peptides,
pubmed-meshheading:15591063-Plasmids,
pubmed-meshheading:15591063-Protein Binding,
pubmed-meshheading:15591063-Protein Structure, Tertiary,
pubmed-meshheading:15591063-Recombinant Fusion Proteins,
pubmed-meshheading:15591063-Ryanodine,
pubmed-meshheading:15591063-Ryanodine Receptor Calcium Release Channel,
pubmed-meshheading:15591063-Scorpion Venoms,
pubmed-meshheading:15591063-Transfection
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pubmed:year |
2005
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pubmed:articleTitle |
Maurocalcine and domain A of the II-III loop of the dihydropyridine receptor Cav 1.1 subunit share common binding sites on the skeletal ryanodine receptor.
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pubmed:affiliation |
INSERM U607/DRDC, CEA, 17 rue des Martyrs, 38054 Grenoble Cedex 09, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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