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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
2009-6-30
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pubmed:abstractText |
Visualizing conformational dynamics in proteins has been difficult, and the atomic-scale motions responsible for the behavior of most allosteric proteins are unknown. Here we report that fluorescence resonance energy transfer (FRET) between a small fluorescent dye and a nickel ion bound to a dihistidine motif can be used to monitor small structural rearrangements in proteins. This method provides several key advantages over classical FRET, including the ability to measure the dynamics of close-range interactions, the use of small probes with short linkers, a low orientation dependence, and the ability to add and remove unique tunable acceptors. We used this 'transition metal ion FRET' approach along with X-ray crystallography to determine the structural changes of the gating ring of the mouse hyperpolarization-activated cyclic nucleotide-regulated ion channel HCN2. Our results suggest a general model for the conformational switch in the cyclic nucleotide-binding site of cyclic nucleotide-regulated ion channels.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19525958-1061067,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19525958-10679227,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19525958-10835104,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19525958-11988471,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19525958-12968185,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19525958-12970756,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19525958-1369354,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19525958-15299374,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19525958-15299926,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19525958-15572765,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19525958-15692043,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19525958-16288781,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19525958-16452984,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/19525958-16622184,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/19525958-17164524,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/19525958-17562314,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/19525958-17766346,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/19525958-18634834,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/19525958-7787045
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1548-7105
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
532-7
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pubmed:dateRevised |
2011-9-26
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pubmed:meshHeading |
pubmed-meshheading:19525958-Amino Acid Sequence,
pubmed-meshheading:19525958-Animals,
pubmed-meshheading:19525958-Binding Sites,
pubmed-meshheading:19525958-Cations, Divalent,
pubmed-meshheading:19525958-Crystallography, X-Ray,
pubmed-meshheading:19525958-Cyclic AMP,
pubmed-meshheading:19525958-Fluorescence Resonance Energy Transfer,
pubmed-meshheading:19525958-Ion Channels,
pubmed-meshheading:19525958-Mice,
pubmed-meshheading:19525958-Models, Molecular,
pubmed-meshheading:19525958-Molecular Sequence Data,
pubmed-meshheading:19525958-Nickel,
pubmed-meshheading:19525958-Peptides,
pubmed-meshheading:19525958-Protein Binding,
pubmed-meshheading:19525958-Protein Conformation,
pubmed-meshheading:19525958-Protein Structure, Secondary,
pubmed-meshheading:19525958-Proteins
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pubmed:year |
2009
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pubmed:articleTitle |
Mapping the structure and conformational movements of proteins with transition metal ion FRET.
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pubmed:affiliation |
Department of Physiology and Biophysics, Howard Hughes Medical Institute, University of Washington, Seattle, Washington, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Evaluation Studies,
Research Support, N.I.H., Extramural
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