| pubmed-article:12169624 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12169624 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:12169624 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:12169624 | lifeskim:mentions | umls-concept:C0031684 | lld:lifeskim |
| pubmed-article:12169624 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:12169624 | lifeskim:mentions | umls-concept:C1522290 | lld:lifeskim |
| pubmed-article:12169624 | lifeskim:mentions | umls-concept:C1335204 | lld:lifeskim |
| pubmed-article:12169624 | lifeskim:mentions | umls-concept:C1418440 | lld:lifeskim |
| pubmed-article:12169624 | lifeskim:mentions | umls-concept:C0600499 | lld:lifeskim |
| pubmed-article:12169624 | lifeskim:mentions | umls-concept:C1719039 | lld:lifeskim |
| pubmed-article:12169624 | lifeskim:mentions | umls-concept:C0220905 | lld:lifeskim |
| pubmed-article:12169624 | pubmed:issue | 16 | lld:pubmed |
| pubmed-article:12169624 | pubmed:dateCreated | 2002-8-9 | lld:pubmed |
| pubmed-article:12169624 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12169624 | pubmed:abstractText | 3-phosphoinositide dependent protein kinase-1 (PDK1) plays a key role in regulating signalling pathways by activating AGC kinases such as PKB/Akt and S6K. Here we describe the 2.0 A crystal structure of the PDK1 kinase domain in complex with ATP. The structure defines the hydrophobic pocket termed the "PIF-pocket", which plays a key role in mediating the interaction and phosphorylation of certain substrates such as S6K1. Phosphorylation of S6K1 at its C-terminal PIF-pocket-interacting motif promotes the binding of S6K1 with PDK1. In the PDK1 structure, this pocket is occupied by a crystallographic contact with another molecule of PDK1. Interestingly, close to the PIF-pocket in PDK1, there is an ordered sulfate ion, interacting tightly with four surrounding side chains. The roles of these residues were investigated through a combination of site-directed mutagenesis and kinetic studies, the results of which confirm that this region of PDK1 represents a phosphate-dependent docking site. We discuss the possibility that an analogous phosphate-binding regulatory motif may participate in the activation of other AGC kinases. Furthermore, the structure of PDK1 provides a scaffold for the design of specific PDK1 inhibitors. | lld:pubmed |
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| pubmed-article:12169624 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12169624 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12169624 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12169624 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12169624 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12169624 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:12169624 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:12169624 | pubmed:author | pubmed-author:van... | lld:pubmed |
| pubmed-article:12169624 | pubmed:author | pubmed-author:DeakMariaM | lld:pubmed |
| pubmed-article:12169624 | pubmed:author | pubmed-author:AlessiDario... | lld:pubmed |
| pubmed-article:12169624 | pubmed:author | pubmed-author:LizcanoJose... | lld:pubmed |
| pubmed-article:12169624 | pubmed:author | pubmed-author:BiondiRicardo... | lld:pubmed |
| pubmed-article:12169624 | pubmed:author | pubmed-author:KomanderDavid... | lld:pubmed |
| pubmed-article:12169624 | pubmed:author | pubmed-author:ThomasChristi... | lld:pubmed |
| pubmed-article:12169624 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12169624 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:12169624 | pubmed:volume | 21 | lld:pubmed |
| pubmed-article:12169624 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12169624 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12169624 | pubmed:pagination | 4219-28 | lld:pubmed |
| pubmed-article:12169624 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:12169624 | pubmed:meshHeading | pubmed-meshheading:12169624... | lld:pubmed |
| pubmed-article:12169624 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12169624 | pubmed:articleTitle | High resolution crystal structure of the human PDK1 catalytic domain defines the regulatory phosphopeptide docking site. | lld:pubmed |
| pubmed-article:12169624 | pubmed:affiliation | Division of Signal Transduction Therapy, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK. | lld:pubmed |
| pubmed-article:12169624 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12169624 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:5170 | entrezgene:pubmed | pubmed-article:12169624 | lld:entrezgene |
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