1kwp
From Proteopedia
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|PDB= 1kwp |SIZE=350|CAPTION= <scene name='initialview01'>1kwp</scene>, resolution 2.8Å | |PDB= 1kwp |SIZE=350|CAPTION= <scene name='initialview01'>1kwp</scene>, resolution 2.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=HG:MERCURY (II) ION'>HG</scene> | + | |LIGAND= <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kwp OCA], [http://www.ebi.ac.uk/pdbsum/1kwp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kwp RCSB]</span> | ||
}} | }} | ||
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[[Category: Meng, W.]] | [[Category: Meng, W.]] | ||
[[Category: Swenson, L L.]] | [[Category: Swenson, L L.]] | ||
| - | [[Category: HG]] | ||
[[Category: crystallography]] | [[Category: crystallography]] | ||
[[Category: mapkap2]] | [[Category: mapkap2]] | ||
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[[Category: signal transduction]] | [[Category: signal transduction]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:54:40 2008'' |
Revision as of 18:54, 30 March 2008
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| , resolution 2.8Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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