1JWH

Crystal Structure of Human Protein Kinase CK2 Holoenzyme

Summary for 1JWH

• Entry DOI: 10.2210/pdb1jwh/pdb
• Related: 1DAW 1DAY 1QF8
• Descriptor: Casein kinase II, alpha chain, Casein kinase II beta chain, PHOSPHATE ION, ... (6 entities in total)
• Functional Keywords: casein kinase 2, ck2 holoenzyme, protein kinase ck2, transferase
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 4
• Total formula weight: 131722.44

Authors

Niefind, K.,Guerra, B.,Ermakowa, I.,Issinger, O.G. (deposition date: 2001-09-04, release date: 2002-03-04, Last modification date: 2023-08-16)

Primary citation

Niefind, K.,Guerra, B.,Ermakowa, I.,Issinger, O.G.
Crystal structure of human protein kinase CK2: insights into basic properties of the CK2 holoenzyme.
EMBO J., 20:5320-5331, 2001

PubMed Abstract: The crystal structure of a fully active form of human protein kinase CK2 (casein kinase 2) consisting of two C-terminally truncated catalytic and two regulatory subunits has been determined at 3.1 A resolution. In the CK2 complex the regulatory subunits form a stable dimer linking the two catalytic subunits, which make no direct contact with one another. Each catalytic subunit interacts with both regulatory chains, predominantly via an extended C-terminal tail of the regulatory subunit. The CK2 structure is consistent with its constitutive activity and with a flexible role of the regulatory subunit as a docking partner for various protein kinases. Furthermore it shows an inter-domain mobility in the catalytic subunit known to be functionally important in protein kinases and detected here for the first time directly within one crystal structure.

PubMed: 11574463
DOI: 10.1093/emboj/20.19.5320

Experimental method

X-RAY DIFFRACTION (3.1 Å)