| pubmed-article:18178622 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18178622 | lifeskim:mentions | umls-concept:C0010531 | lld:lifeskim |
| pubmed-article:18178622 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:18178622 | pubmed:dateCreated | 2008-1-16 | lld:pubmed |
| pubmed-article:18178622 | pubmed:abstractText | Allosteric signaling in proteins requires long-range communication mediated by highly conserved residues, often triggered by ligand binding. In this article, we map the allosteric network in the catalytic subunit of protein kinase A using NMR spectroscopy. We show that positive allosteric cooperativity is generated by nucleotide and substrate binding during the transitions through the major conformational states: apo, intermediate, and closed. The allosteric network is disrupted by a single site mutation (Y204A), which also decouples the cooperativity of ligand binding. Because protein kinase A is the prototype for the entire kinome, these findings may serve as a paradigm for describing long-range coupling in other protein kinases. | lld:pubmed |
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| pubmed-article:18178622 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:18178622 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:18178622 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18178622 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:18178622 | pubmed:issn | 1091-6490 | lld:pubmed |
| pubmed-article:18178622 | pubmed:author | pubmed-author:TaylorSusan... | lld:pubmed |
| pubmed-article:18178622 | pubmed:author | pubmed-author:MascioniAless... | lld:pubmed |
| pubmed-article:18178622 | pubmed:author | pubmed-author:VegliaGianlui... | lld:pubmed |
| pubmed-article:18178622 | pubmed:author | pubmed-author:TraasethNatha... | lld:pubmed |
| pubmed-article:18178622 | pubmed:author | pubmed-author:MastersonLarr... | lld:pubmed |
| pubmed-article:18178622 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18178622 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:18178622 | pubmed:volume | 105 | lld:pubmed |
| pubmed-article:18178622 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18178622 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18178622 | pubmed:pagination | 506-11 | lld:pubmed |
| pubmed-article:18178622 | pubmed:dateRevised | 2011-3-14 | lld:pubmed |
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