Protein kinase MK2 in complex with an inhibitor (crystal form-2, co- crystallization)

Structural basis for a high affinity inhibitor bound to protein kinase MK2.

Identifying Protein Construct Variants with Increased Crystallization Propensity-A Case Study.

MAPKAP KINASE 2, MAPK-ACTIVATED PROTEIN KINASE 2, MAPKAPK-2, MK2

MOLREP IDENTIFIED 11 MOLECULES. AFTER SOME REBUILDING AND REFINEMENT, BEAST IDENTIFIED THE TWELTH MOLECULE.

1.8-2.0M SODIUM POTTASIUM PHOSPHATE PH 7.5, 0.0003M INHIBITOR

CRYSTAL STRUCTURE OF STAUROSPORINE BOUND TO MAP KAP KINASE 2

CRYSTAL STRUCTURE OF ADP BOUND TO MAP KAP KINASE 2

PROTEIN KINASE MK2 IN COMPLEX WITH AN INHIBITOR (CRYSTAL FORM-1, SOAKING)

SHEET
THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
TWO SHEETS ARE DEFINED.

2-(QUINOLIN-3-YLPYRIDIN-4-YL)-1,5,6,
7-TETRAHYDRO-4H-PYRROLO[3,2-C]PYRIDIN-4-ONE (P4O): PROTEIN
CHAIN J HAS NO LIGAND BOUND IN THE ACTIVE SITE, THEREFORE
THERE IS NO LIGAND J, AND IN TOTAL THERE ARE ONLY 11
LIGAND MOLECULES.

N-TERMINAL RESIDUES GLY-SER ARE CLONING ARTEFACTS FROM A THROMBIN CLEAVAGE SITE, AFTER GST TAG CLEAVAGE.

IN THE CRYSTAL LATTICE, THE TWELVE MK2 MOLECULES FORM FOUR TRIMERS OF TYPE-1, VIA N-TERMINI, AND THREE TRIMERS OF TYPE-2, VIA ACTIVATION SEGMENTS. THE ACTIVATION SEGMENTS INCLUDE RESIDUES 207 - 233 AND ARE PARTIALLY DISORDERED.
MAP KINASE-ACTIVATED PROTEIN KINASE 2 (E.C.2.7.11.1)
SER-THR KINASE, MAPKAP KINASE 2, PHOSPHORYLATION, SMALL MOLECULE INHIBITOR, MK2, KINASE, ATP SITE, TRANSFERASE, ATP- BINDING, SERINE/THREONINE-PROTEIN KINASE, CO-CRYSTALLIZATION, NUCLEOTIDE-BINDING