Structure of CDK9 in complex with cyclin T and a 2-amino-4-heteroaryl- pyrimidine inhibitor

Comparative Structural and Functional Studies of 4-(Thiazol- 5-Yl)-2-(Phenylamino)Pyrimidine-5-Carbonitrile Cdk9 Inhibitors Suggest the Basis for Isotype Selectivity.

C-2K, CELL DIVISION CYCLE 2-LIKE PROTEIN KINASE 4, CELL DIVISION PROTEIN KINASE 9, SERINE/THREONINE-PROTEIN KINASE PITALRE, TAT-ASSOCIATED KINASE COMPLEX CATALYTIC SUBUNIT

CRYSTALS WERE GROWN AT 4C USING 10-16% PEG 1000, 100MM NAK-PHOSPHATE PH 6.2, 500MM NACL, 4MM TCEP AS THE PRECIPITANT SOLUTION. THEY WERE SUBSEQUENTLY SOAKED IN THE PRESENCE OF COMPOUND.

STRUCTURE OF CDK9 IN COMPLEX WITH CYCLIN T AND A 2 -AMINO-4-HETEROARYL-PYRIMIDINE INHIBITOR

STRUCTURE OF CDK2 IN COMPLEX WITH CYCLIN A AND A 2 -AMINO-4-HETEROARYL-PYRIMIDINE INHIBITOR

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.

CYCLIN-DEPENDENT KINASE 9 (E.C.2.7.11.22, 2.7.11.23), CYCLIN-T1

TRANSFERASE-CELL CYCLE COMPLEX, CDK-CYCLIN COMPLEX, TRANSCRIPTION-PROTEIN BINDING, STRUCTURE-BASED DRUG DESIGN