2okr: Difference between revisions

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==Overview==

The p38 signaling pathway is activated in response to cell stress and, induces production of proinflammatory cytokines. P38alpha is, phosphorylated and activated in response to cell stress by MKK3 and MKK6, and in turn phosphorylates a number of substrates, including MAPKAP kinase, 2 (MK2). We have determined the crystal structure of the unphosphorylated, p38alpha-MK2 heterodimer. The C-terminal regulatory domain of MK2 binds in, the docking groove of p38alpha and the ATP-binding sites of both kinases, are at the heterodimer interface. The conformation suggests an extra, mechanism in addition to the regulation of the p38alpha and MK2, phosphorylation states that prevents phosphorylation of substrates in the, absence of cell stress. Addition of constitutively active MKK6-DD results, in rapid phosphorylation of the p38alpha-MK2 heterodimer.

The p38 signaling pathway is activated in response to cell stress and induces production of proinflammatory cytokines. P38alpha is phosphorylated and activated in response to cell stress by MKK3 and MKK6 and in turn phosphorylates a number of substrates, including MAPKAP kinase 2 (MK2). We have determined the crystal structure of the unphosphorylated p38alpha-MK2 heterodimer. The C-terminal regulatory domain of MK2 binds in the docking groove of p38alpha, and the ATP-binding sites of both kinases are at the heterodimer interface. The conformation suggests an extra mechanism in addition to the regulation of the p38alpha and MK2 phosphorylation states that prevents phosphorylation of substrates in the absence of cell stress. Addition of constitutively active MKK6-DD results in rapid phosphorylation of the p38alpha-MK2 heterodimer.

==About this Structure==

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==Reference==

Crystal structure of the ~~p38alpha~~ -MAPKAP kinase 2 heterodimer., ~~Ter~~ Haar E, ~~Prabakhar~~ P, Liu X, Lepre C, J Biol Chem. 2007 Jan 25;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17255097 17255097]

Crystal structure of the p38 alpha-MAPKAP kinase 2 heterodimer., ter Haar E, Prabhakar P, Liu X, Lepre C, J Biol Chem. 2007 Mar 30;282(13):9733-9. Epub 2007 Jan 25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17255097 17255097]

[[Category: Homo sapiens]]

[[Category: Mitogen-activated protein kinase]]

[[Category: Protein complex]]

[[Category: Haar, E.Ter.]]

[[Category: Haar, E Ter.]]

[[Category: docking groove]]

[[Category: heterodimer]]

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[[Category: nls]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-The p38 signaling pathway is activated in response to cell stress and, induces production of proinflammatory cytokines. P38alpha is, phosphorylated and activated in response to cell stress by MKK3 and MKK6, and in turn phosphorylates a number of substrates, including MAPKAP kinase, 2 (MK2). We have determined the crystal structure of the unphosphorylated, p38alpha-MK2 heterodimer. The C-terminal regulatory domain of MK2 binds in, the docking groove of p38alpha and the ATP-binding sites of both kinases, are at the heterodimer interface. The conformation suggests an extra, mechanism in addition to the regulation of the p38alpha and MK2, phosphorylation states that prevents phosphorylation of substrates in the, absence of cell stress. Addition of constitutively active MKK6-DD results, in rapid phosphorylation of the p38alpha-MK2 heterodimer.
+The p38 signaling pathway is activated in response to cell stress and induces production of proinflammatory cytokines. P38alpha is phosphorylated and activated in response to cell stress by MKK3 and MKK6 and in turn phosphorylates a number of substrates, including MAPKAP kinase 2 (MK2). We have determined the crystal structure of the unphosphorylated p38alpha-MK2 heterodimer. The C-terminal regulatory domain of MK2 binds in the docking groove of p38alpha, and the ATP-binding sites of both kinases are at the heterodimer interface. The conformation suggests an extra mechanism in addition to the regulation of the p38alpha and MK2 phosphorylation states that prevents phosphorylation of substrates in the absence of cell stress. Addition of constitutively active MKK6-DD results in rapid phosphorylation of the p38alpha-MK2 heterodimer.
 ==About this Structure==
@@ Line 10: / Line 10: @@
 ==Reference==
-Crystal structure of the p38alpha -MAPKAP kinase 2 heterodimer., Ter Haar E, Prabakhar P, Liu X, Lepre C, J Biol Chem. 2007 Jan 25;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17255097 17255097]
+Crystal structure of the p38 alpha-MAPKAP kinase 2 heterodimer., ter Haar E, Prabhakar P, Liu X, Lepre C, J Biol Chem. 2007 Mar 30;282(13):9733-9. Epub 2007 Jan 25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17255097 17255097]
 [[Category: Homo sapiens]]
 [[Category: Mitogen-activated protein kinase]]
 [[Category: Protein complex]]
-[[Category: Haar, E.Ter.]]
+[[Category: Haar, E Ter.]]
 [[Category: docking groove]]
 [[Category: heterodimer]]
@@ Line 21: / Line 21: @@
 [[Category: nls]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:32:30 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:19:33 2008''