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Literature summary for 2.7.11.24 extracted from

  • ter Haar, E.; Prabhakar, P.; Prabakhar, P.; Liu, X.; Lepre, C.
    Crystal structure of the p38 alpha-MAPKAP kinase 2 heterodimer (2007), J. Biol. Chem., 282, 9733-9739.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information MKK6-DD phosphorylates the p38a-MK2 heterodimer Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of the unphosphorylated p38alpha-MK2, by hanging drop method, full-length p38alpha-MK2 complex to 4 A resolution, belongs to spacegroup P41 with unit cell dimensions of 103.09 A, 103.09 A, 231.42 A, 90.0°, 90.0°, 90.0°, p38alpha-MK2 peptide complex, belongs to spacegroup P31 with unit cell dimensions of 81.55 A, 81.55 A, 121.36 A, 90.0°, 90.0°, 120.0°. 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 Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
SB203580 inhibits MK2 phosphorylation Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
gel filtration Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + MK2
-
Homo sapiens ADP + phosphorylated MK2
-
?

Synonyms

Synonyms Comment Organism
P38alpha-MAPKAP kinase 2
-
Homo sapiens