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rdf:type |
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lifeskim:mentions |
umls-concept:C0020275,
umls-concept:C0033684,
umls-concept:C0392747,
umls-concept:C0425245,
umls-concept:C0442726,
umls-concept:C0443172,
umls-concept:C0521119,
umls-concept:C0678640,
umls-concept:C0851285,
umls-concept:C1511790,
umls-concept:C1879547
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pubmed:issue |
3
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pubmed:dateCreated |
2001-2-22
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pubmed:abstractText |
Changes in protein mobility accompany changes in conformation during the trans-activation of enzymes; however, few studies exist that validate or characterize this behavior. In this study, amide hydrogen/deuterium exchange/mass spectrometry was used to probe the conformational flexibility of extracellular signal-regulated protein kinase-2 before and after activation by phosphorylation. The exchange data indicated that extracellular regulated protein kinase-2 activation caused altered backbone flexibility in addition to the conformational changes previously established by x-ray crystallography. The changes in flexibility occurred in regions involved in substrate binding and turnover, suggesting their importance in enzyme regulation.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11158577-10064715,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11158577-10207078,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11158577-10439507,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11158577-10452602,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11158577-10454192,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11158577-10479734,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11158577-15299354,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11158577-1862343,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11158577-2010918,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11158577-3051385,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11158577-7712287,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11158577-7712293,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11158577-7756994,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11158577-7937704,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11158577-8001819,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11158577-8081750,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11158577-8107865,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11158577-8202162,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11158577-8234246,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11158577-8444886,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11158577-8528084,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11158577-8538461,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11158577-8547258,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11158577-8612268,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11158577-8836096,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11158577-8876652,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11158577-9054567,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11158577-9261084,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11158577-9298898,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11158577-9425067,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11158577-9519304,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11158577-9541406,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11158577-9604935,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11158577-9827991
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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 |
Jan
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
98
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
956-61
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11158577-Adenosine Triphosphate,
pubmed-meshheading:11158577-Animals,
pubmed-meshheading:11158577-Binding Sites,
pubmed-meshheading:11158577-Hydrogen Bonding,
pubmed-meshheading:11158577-Ligands,
pubmed-meshheading:11158577-Mitogen-Activated Protein Kinase 1,
pubmed-meshheading:11158577-Models, Molecular,
pubmed-meshheading:11158577-Peptide Fragments,
pubmed-meshheading:11158577-Phosphorylation,
pubmed-meshheading:11158577-Protein Conformation,
pubmed-meshheading:11158577-Protein Structure, Secondary,
pubmed-meshheading:11158577-Rats,
pubmed-meshheading:11158577-Recombinant Proteins
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pubmed:year |
2001
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pubmed:articleTitle |
Changes in protein conformational mobility upon activation of extracellular regulated protein kinase-2 as detected by hydrogen exchange.
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pubmed:affiliation |
Department of Chemistry and Biochemistry, and Howard Hughes Medical Institute, University of Colorado, Boulder, CO 80309, USA. ahn@spot.colorado.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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