1kwp

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(New page: 200px<br /> <applet load="1kwp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kwp, resolution 2.8&Aring;" /> '''Crystal Structure of...)
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<applet load="1kwp" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1kwp, resolution 2.8&Aring;" />
caption="1kwp, resolution 2.8&Aring;" />
'''Crystal Structure of MAPKAP2'''<br />
'''Crystal Structure of MAPKAP2'''<br />
==Overview==
==Overview==
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MAPK-activated protein kinase 2 (MAPKAPK2), one of several kinases, directly phosphorylated and activated by p38 MAPK, plays a central role in, the inflammatory response. The activated MAPKAPK2 phosphorylates its, nuclear targets CREB/ATF1, serum response factor, and E2A protein E47 and, its cytoplasmic targets HSP25/27, LSP-1, 5-lipoxygenase, glycogen, synthase, and tyrosine hydroxylase. The crystal structure of, unphosphorylated MAPKAPK2, determined at 2.8 A resolution, includes the, kinase domain and the C-terminal regulatory domain. Although the protein, is inactive, the kinase domain adopts an active conformation with, aspartate 366 mimicking the missing phosphorylated threonine 222 in the, activation loop. The C-terminal regulatory domain forms a helix-turn-helix, plus a long strand. Phosphorylation of threonine 334, which is located, between the kinase domain and the C-terminal regulatory domain, may serve, as a switch for MAPKAPK2 nuclear import and export. Phosphorylated, MAPKAPK2 masks the nuclear localization signal at its C terminus by, binding to p38. It unmasks the nuclear export signal, which is part of the, second C-terminal helix packed along the surface of kinase domain C-lobe, and thereby carries p38 to the cytoplasm.
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MAPK-activated protein kinase 2 (MAPKAPK2), one of several kinases directly phosphorylated and activated by p38 MAPK, plays a central role in the inflammatory response. The activated MAPKAPK2 phosphorylates its nuclear targets CREB/ATF1, serum response factor, and E2A protein E47 and its cytoplasmic targets HSP25/27, LSP-1, 5-lipoxygenase, glycogen synthase, and tyrosine hydroxylase. The crystal structure of unphosphorylated MAPKAPK2, determined at 2.8 A resolution, includes the kinase domain and the C-terminal regulatory domain. Although the protein is inactive, the kinase domain adopts an active conformation with aspartate 366 mimicking the missing phosphorylated threonine 222 in the activation loop. The C-terminal regulatory domain forms a helix-turn-helix plus a long strand. Phosphorylation of threonine 334, which is located between the kinase domain and the C-terminal regulatory domain, may serve as a switch for MAPKAPK2 nuclear import and export. Phosphorylated MAPKAPK2 masks the nuclear localization signal at its C terminus by binding to p38. It unmasks the nuclear export signal, which is part of the second C-terminal helix packed along the surface of kinase domain C-lobe, and thereby carries p38 to the cytoplasm.
==About this Structure==
==About this Structure==
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1KWP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with HG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KWP OCA].
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1KWP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=HG:'>HG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KWP OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Behrens, A.E.]]
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[[Category: Behrens, A E.]]
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[[Category: Fitzgibbon, M.J.]]
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[[Category: Fitzgibbon, M J.]]
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[[Category: Fulghum, J.R.]]
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[[Category: Fulghum, J R.]]
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[[Category: Haar, E.ter.]]
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[[Category: Haar, E ter.]]
[[Category: Hayakawa, K.]]
[[Category: Hayakawa, K.]]
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[[Category: Lippke, J.A.]]
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[[Category: Lippke, J A.]]
[[Category: Meng, W.]]
[[Category: Meng, W.]]
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[[Category: Swenson, L.L.]]
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[[Category: Swenson, L L.]]
[[Category: HG]]
[[Category: HG]]
[[Category: crystallography]]
[[Category: crystallography]]
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[[Category: signal transduction]]
[[Category: signal transduction]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:55:31 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:38:45 2008''

Revision as of 11:38, 21 February 2008


1kwp, resolution 2.8Å

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Crystal Structure of MAPKAP2

Overview

MAPK-activated protein kinase 2 (MAPKAPK2), one of several kinases directly phosphorylated and activated by p38 MAPK, plays a central role in the inflammatory response. The activated MAPKAPK2 phosphorylates its nuclear targets CREB/ATF1, serum response factor, and E2A protein E47 and its cytoplasmic targets HSP25/27, LSP-1, 5-lipoxygenase, glycogen synthase, and tyrosine hydroxylase. The crystal structure of unphosphorylated MAPKAPK2, determined at 2.8 A resolution, includes the kinase domain and the C-terminal regulatory domain. Although the protein is inactive, the kinase domain adopts an active conformation with aspartate 366 mimicking the missing phosphorylated threonine 222 in the activation loop. The C-terminal regulatory domain forms a helix-turn-helix plus a long strand. Phosphorylation of threonine 334, which is located between the kinase domain and the C-terminal regulatory domain, may serve as a switch for MAPKAPK2 nuclear import and export. Phosphorylated MAPKAPK2 masks the nuclear localization signal at its C terminus by binding to p38. It unmasks the nuclear export signal, which is part of the second C-terminal helix packed along the surface of kinase domain C-lobe, and thereby carries p38 to the cytoplasm.

About this Structure

1KWP is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Structure of mitogen-activated protein kinase-activated protein (MAPKAP) kinase 2 suggests a bifunctional switch that couples kinase activation with nuclear export., Meng W, Swenson LL, Fitzgibbon MJ, Hayakawa K, Ter Haar E, Behrens AE, Fulghum JR, Lippke JA, J Biol Chem. 2002 Oct 4;277(40):37401-5. Epub 2002 Aug 8. PMID:12171911

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