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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 1
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pubmed:dateCreated |
2006-3-1
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pubmed:abstractText |
AMP-activated protein kinase (AMPK) is an intracellular energy sensor that regulates metabolism in response to energy demand and supply by adjusting the ATP-generating and ATP-consuming pathways. AMPK potentially plays a critical role in diabetes and obesity as it is known to be activated by metforin and rosiglitazone, drugs used for the treatment of type II diabetes. AMPK is a heterotrimer composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. Mutations in the gamma subunit are known to cause glycogen accumulation, leading to cardiac arrhythmias. Recently, a functional glycogen-binding domain (GBD) has been identified in the beta subunit. Here, the crystallization of GBD in the presence of beta-cyclodextrin is reported together with preliminary X-ray data analysis allowing the determination of the structure by single isomorphous replacement and threefold averaging using in-house X-ray data collected from a selenomethionine-substituted protein.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16508085-10087918,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16508085-10544261,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16508085-11994296,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16508085-12015471,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16508085-12747836,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16508085-12747837,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16508085-12829246,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16508085-12930991,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16508085-14614828,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16508085-14722619,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16508085-14729328,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16508085-15299374,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16508085-5700707,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16508085-9195884
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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 |
1744-3091
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
61
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
39-42
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:16508085-AMP-Activated Protein Kinases,
pubmed-meshheading:16508085-Animals,
pubmed-meshheading:16508085-Binding Sites,
pubmed-meshheading:16508085-Cloning, Molecular,
pubmed-meshheading:16508085-Crystallization,
pubmed-meshheading:16508085-DNA Primers,
pubmed-meshheading:16508085-Glycogen,
pubmed-meshheading:16508085-Multienzyme Complexes,
pubmed-meshheading:16508085-Peptide Fragments,
pubmed-meshheading:16508085-Protein Kinases,
pubmed-meshheading:16508085-Protein Subunits,
pubmed-meshheading:16508085-Protein-Serine-Threonine Kinases,
pubmed-meshheading:16508085-Rats,
pubmed-meshheading:16508085-Recombinant Proteins,
pubmed-meshheading:16508085-Selenomethionine,
pubmed-meshheading:16508085-X-Ray Diffraction
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pubmed:year |
2005
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pubmed:articleTitle |
Crystallization of the glycogen-binding domain of the AMP-activated protein kinase beta subunit and preliminary X-ray analysis.
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pubmed:affiliation |
St Vincent's Institute of Medical Research, Fitzroy, Victoria 3065, Australia. gpolekhina@svi.edu.au
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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