forked from D-Net/dnet-hadoop
1030 lines
31 KiB
JSON
1030 lines
31 KiB
JSON
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"abstract": "<jats:p>Glycogen synthase kinase-3 (GSK-3) is a key regulator of many cellular signaling pathways. Unlike most kinases, GSK-3 is controlled by inhibition rather than by specific activation. In the insulin and several other signaling pathways, phosphorylation of a serine present in a conserved sequence near the amino terminus of GSK-3 generates an auto-inhibitory peptide. In contrast, Wnt\/\u03b2-catenin signal transduction requires phosphorylation of Ser\/Pro rich sequences present in the Wnt co-receptors LRP5\/6, and these motifs inhibit GSK-3 activity. We present crystal structures of GSK-3 bound to its phosphorylated N-terminus and to two of the phosphorylated LRP6 motifs. A conserved loop unique to GSK-3 undergoes a dramatic conformational change that clamps the bound pseudo-substrate peptides, and reveals the mechanism of primed substrate recognition. The structures rationalize target sequence preferences and suggest avenues for the design of inhibitors selective for a subset of pathways regulated by GSK-3.<\/jats:p>",
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"DOI": "10.7554\/elife.01998",
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"title": [
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"Structural basis of GSK-3 inhibition by N-terminal phosphorylation and by the Wnt receptor LRP6"
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"name": "Department of Structural Biology, Stanford University, Stanford, United States"
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{
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"name": "Department of Molecular and Cellular Physiology, Stanford University, Stanford, United States"
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"given": "Matthew Ling-Hon",
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"name": "Department of Structural Biology, Stanford University, Stanford, United States"
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"name": "Department of Molecular and Cellular Physiology, Stanford University, Stanford, United States"
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|
"name": "accepted",
|
|
"label": "Accepted",
|
|
"group": {
|
|
"name": "publication_history",
|
|
"label": "Publication History"
|
|
}
|
|
},
|
|
{
|
|
"value": "2014-03-18",
|
|
"order": 2,
|
|
"name": "published",
|
|
"label": "Published",
|
|
"group": {
|
|
"name": "publication_history",
|
|
"label": "Publication History"
|
|
}
|
|
}
|
|
]
|
|
}
|