6HNW

Human protein kinase CK2 alpha in complex with coumestrol

Summary for 6HNW

Entry DOI	10.2210/pdb6hnw/pdb
Descriptor	Casein kinase II subunit alpha, Coumestrol, SULFATE ION, ... (4 entities in total)
Functional Keywords	kinase domain, transferase
Biological source	Homo sapiens (Human)
Total number of polymer chains	1
Total formula weight	40614.17
Authors	Battistutta, R.,Lolli, G. (deposition date: 2018-09-17, release date: 2019-08-07, Last modification date: 2024-01-24)
Primary citation	Battistutta, R.,Lolli, G. Inhibitory Properties of ATP-Competitive Coumestrol and Boldine Are Correlated to Different Modulations of CK2 Flexibility. J.Nat.Prod., 82:1014-1018, 2019 Cited by PubMed Abstract: Casein kinase 2 (CK2) is an anti-apoptotic cancer-sustaining protein kinase. Its crystallographic structures with the natural compounds coumestrol, a phytoestrogen, and boldine, an alkaloid, are reported. Coumestrol shows different inhibitory activity against the isolated catalytic α-subunit and the αβ holoenzyme and is able to discriminate between two conformations of the hinge/αD region, whose intrinsic flexibility is a relevant selectivity determinant among kinases. Boldine explores a small cavity at the bottom of the ATP-binding pocket through a local deviation from planarity, a unique case among CK2 inhibitors. The two compounds have different impacts on protein flexibility, which correlate with their different properties. PubMed: 30840451 DOI: 10.1021/acs.jnatprod.8b00889 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2 Å)

Structure validation