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Literature summary for 2.7.12.2 extracted from

  • Matsumoto, T.; Kinoshita, T.; Kirii, Y.; Tada, T.; Yamano, A.
    Crystal and solution structures disclose a putative transient state of mitogen-activated protein kinase kinase 4 (2012), Biochem. Biophys. Res. Commun., 425, 195-200.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant apo MAP2K4-KD or in complex with ANP, 15 mg/ml protein in a solution containing 20 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10% glycerol and 10 mM DTT for the apoenzyme, and 2 mM ANP and MgCl2 additional for the npMAP2K4/ANP complex, mixing with reservoir solution containing 0.2 M ammonium acetate, 22-25% w/v PEG 3350 and 0.1 M HEPES–NaOH, pH 7.0, 20°C, X-ray diffraction structure determination and analysis at 3.5 A resolution Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
37950
-
-
Homo sapiens
39000
-
-
Homo sapiens
40000
-
-
Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P45985
-
-

Subunits

Subunits Comment Organism
? x * 37419 , apo npMAP2K4, sequence calculation, x * 37950, npMAP2K4/ANP complex, sequence calculation, x * 39000 , apo npMAP2K4, light scattering, x * 40000, npMAP2K4/ANP complex, light scattering Homo sapiens

Synonyms

Synonyms Comment Organism
MAP2K4
-
Homo sapiens
mitogen-activated protein kinase kinase 4
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP upon ATP-binding, the transient conformation adopted the configuration of typical kinase folding. In the absence of ATP-binding, the transient state of apo npMAP2K4 may shift to a state of aggregation via non-particular hydrophobic interactions as a result of the exposed hydrophobic residues Homo sapiens

General Information

General Information Comment Organism
additional information the transient state of apo npMAP2K4 exists between the canonical kinase fold and the aggregation state. The ATP molecule under physiological conditions allows the transient conformation to rapidly assume the canonical kinase fold but the depletion of ATP under conditions of low levels of bioactivity perhaps enhances the transition to the aggregation state Homo sapiens
physiological function mitogen-activated protein kinase kinase 4 (MAP2K4) plays a crucial role in the stress-activated signal cascade and is enzymatically regulated by ligand or substrate binding, and/or post-translational modification Homo sapiens