2fys
From Proteopedia
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| - | [[Image:2fys.gif|left|200px]] | + | [[Image:2fys.gif|left|200px]] |
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| - | '''Crystal structure of Erk2 complex with KIM peptide derived from MKP3''' | + | {{Structure |
| + | |PDB= 2fys |SIZE=350|CAPTION= <scene name='initialview01'>2fys</scene>, resolution 2.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] | ||
| + | |GENE= Mapk1, Erk2, Mapk, Prkm1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of Erk2 complex with KIM peptide derived from MKP3''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2FYS is a [ | + | 2FYS is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FYS OCA]. |
==Reference== | ==Reference== | ||
| - | Structural basis of docking interactions between ERK2 and MAP kinase phosphatase 3., Liu S, Sun JP, Zhou B, Zhang ZY, Proc Natl Acad Sci U S A. 2006 Apr 4;103(14):5326-31. Epub 2006 Mar 27. PMID:[http:// | + | Structural basis of docking interactions between ERK2 and MAP kinase phosphatase 3., Liu S, Sun JP, Zhou B, Zhang ZY, Proc Natl Acad Sci U S A. 2006 Apr 4;103(14):5326-31. Epub 2006 Mar 27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16567630 16567630] |
[[Category: Non-specific serine/threonine protein kinase]] | [[Category: Non-specific serine/threonine protein kinase]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: mkp3]] | [[Category: mkp3]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:58:26 2008'' |
Revision as of 14:58, 20 March 2008
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| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | Mapk1, Erk2, Mapk, Prkm1 (Rattus norvegicus) | ||||||
| Activity: | Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of Erk2 complex with KIM peptide derived from MKP3
Overview
Mitogen-activated protein (MAP) kinases are central components of signal transduction pathways for cell proliferation, stress responses, and differentiation. Signaling efficiency and specificity are modulated in large part by docking interactions between individual MAP kinase and the kinase interaction motif (KIM), (R/K)(2-3)-X(1-6)-Phi(A)-X-Phi(B), in its cognate kinases, phosphatases, scaffolding proteins, and substrates. We have determined the crystal structure of extracellular signal-regulated protein kinase 2 bound to the KIM peptide from MAP kinase phosphatase 3, an extracellular signal-regulated protein kinase 2-specific phosphatase. The structure reveals that the KIM docking site, situated in a noncatalytic region opposite of the kinase catalytic pocket, is comprised of a highly acidic patch and a hydrophobic groove, which engage the basic and Phi(A)-X-Phi(B) residues, respectively, in the KIM sequence. The specific docking interactions observed in the structure consolidate all known biochemical data. In addition, structural comparison indicates that the KIM docking site is conserved in all MAP kinases. The results establish a structural model for understanding how MAP kinases interact with their regulators and substrates and provide new insights into how MAP kinase docking specificity can be achieved.
About this Structure
2FYS is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structural basis of docking interactions between ERK2 and MAP kinase phosphatase 3., Liu S, Sun JP, Zhou B, Zhang ZY, Proc Natl Acad Sci U S A. 2006 Apr 4;103(14):5326-31. Epub 2006 Mar 27. PMID:16567630
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