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Copyright © 2006 by Danielle Shingle & Karl Oberholser,
Messiah College, Grantham PA USA.
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ERK2
ERK2 is a MAP Kinase that phosphorylates transcription factors as well as other kinases. The general structure of ERK2 is shown here.
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Secondary Structure
The secondary structure of this enzyme reveals multiple alpha-helices (magenta) and 2 main locations for the beta sheets(green). Also multiple water molecules are present, and displayed in red.
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Phosphorylation sites
ERK2 has dual phosphorylation sites. Tyrosine 185 is first phosphorylation site on the ERK2 kinase. This site is phosphorylated by MEK1/2
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Phosphorylation sites
ERK2 has dual phosphorylation sites. The threonine residue 183 is the second target of phosphorylation by MEK, the primary kinase that phosphorylates MAP Kinases.
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Conformation Changes in Phosphothreonine
When threonine 183 is phosphorylated its conformation changes to make 8 hydrogen bonds with surrounding Arginine residues. Arg-68 in helix C, Arg-146 in the catalytic loop, Arg-170 in the lip, and Arg-65 in helix C
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Conformation Changes in Phosphotyrosine
Tyrosine-185 is buried within the molecule prior to phosphorylation. After phosphorylation, it rotates around and exposes its side chain to the surface. P-Tyrosine forms 4 interactions, 2 with Arg-189 and 2 with Arg-192, as opposed to the eight seen in phosphothreonine. Allowing this amino acid to expose its side chain to solvents.
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Binding Domain
D316 and D319 (aspartic acids) are the two amino acids involved in forming binding domains for the MEK protein.
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P+1 Binding Site
The substrate binding site on ERK 2 is a pocket located at the C-Terminal Domain
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P+1 binding site
ERK 2 has a specific P+1 binding site for the binding of substrates that it phosphorylates. ERK 2 is specific in that it binds substrates that contain a trans- oriented proline becuase it can bind to Leu-168,pTyr-185, and Ala-187. It is also specific for proline because the binding of other amino acids would cost energy due to there inability to bind with the pTyr-185/Ala-187 backbone.
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