|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
20
|
|
pubmed:dateCreated |
1995-12-21
|
|
pubmed:abstractText |
Calcium is a universally employed cytosolic messenger in eukaryotic cells. Most of the proteins that bind signalling calcium are members of the calmodulin superfamily and share two or more helix-loop-helix motifs known as EF-hands. A model, based on structure comparison of different domains and supported by preliminary NMR data, has suggested that EF-hands involved in signal transduction undergo a major conformational change upon calcium binding from a 'closed' to an 'open' state allowing protein-protein interaction. We have determined the solution structures of the EF-hand pair from alpha-spectrin in the absence and in the presence of calcium. The structures are in the closed and open conformation respectively, providing a definite experimental proof for the closed-to-open model. Our results allow formulation of the rules which govern the movement induced by calcium. These rules may be generalized to other EF-hands since the key residues involved are conserved within the calmodulin family.
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7588621-1303746,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7588621-1490109,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7588621-1519061,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7588621-1585175,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7588621-1737021,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7588621-1841711,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7588621-1847217,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7588621-1854476,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7588621-1960729,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7588621-2183842,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7588621-2200514,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7588621-2268628,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7588621-2673026,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7588621-2819050,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7588621-2910879,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7588621-3949740,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7588621-3969570,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7588621-3990807,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7588621-7656053,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7588621-7703843,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7588621-7851407,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7588621-7971971,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7588621-8262263,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7588621-8450536,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7588621-8486739
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Oct
|
|
pubmed:issn |
0261-4189
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
16
|
|
pubmed:volume |
14
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
4922-31
|
|
pubmed:dateRevised |
2009-11-18
|
|
pubmed:meshHeading |
pubmed-meshheading:7588621-Amino Acid Sequence,
pubmed-meshheading:7588621-Calcium,
pubmed-meshheading:7588621-Computer Simulation,
pubmed-meshheading:7588621-Magnetic Resonance Spectroscopy,
pubmed-meshheading:7588621-Models, Molecular,
pubmed-meshheading:7588621-Molecular Sequence Data,
pubmed-meshheading:7588621-Protein Conformation,
pubmed-meshheading:7588621-Sequence Homology, Amino Acid,
pubmed-meshheading:7588621-Spectrin,
pubmed-meshheading:7588621-Troponin,
pubmed-meshheading:7588621-Troponin C
|
|
pubmed:year |
1995
|
|
pubmed:articleTitle |
Molecular mechanism of the calcium-induced conformational change in the spectrin EF-hands.
|
|
pubmed:affiliation |
European Molecular Biology Laboratory, Heidelberg, Germany.
|
|
pubmed:publicationType |
Journal Article
|
