scholarly journals Crystal structures of human CK2α2 in new crystal forms arising from a subtle difference in salt concentration

2018 ◽  
Vol 74 (5) ◽  
pp. 288-293 ◽  
Author(s):  
Masato Tsuyuguchi ◽  
Tetsuko Nakaniwa ◽  
Takayoshi Kinoshita
Keyword(s):  
Crystal Structure ◽  
Crystal Structures ◽  
Protein Kinase Ck2 ◽  
Selective Inhibitors ◽  
Subtle Difference ◽  
Catalytic Subunits ◽  
Crystal Forms ◽  
Male Contraceptive ◽  
Kinase Ck2 ◽  
Drug Discovery Target

The catalytic subunits of protein kinase CK2 are classified into two subtypes: CK2α1 and CK2α2. CK2α1 is an attractive drug-discovery target for various diseases such as cancers and nephritis. CK2α2 is defined as an off-target of CK2α1 and is a potential target in the development of male contraceptive drugs. High-resolution crystal structures of both isozymes are likely to provide crucial clues for the design of selective inhibitors of CK2α1 and/or CK2α2. To date, several crystal structures of CK2α1 have been solved at high resolutions of beyond 1.5 Å. However, crystal structures of CK2α2 have barely achieved a low resolution of around 3 Å because of the formation of needle-shaped crystals. In this study, new crystal forms were exploited and one provided a crystal structure of CK2α2 at 1.89 Å resolution. This result, together with the structure of CK2α1, will assist in the development of highly selective inhibitors for both isozymes.

The crystal structure of the complex of Zea maysα subunit with a fragment of human β subunit provides the clue to the architecture of protein kinase CK2 holoenzyme

2000 ◽  
Vol 267 (16) ◽  
pp. 5184-5190 ◽  
Author(s):  
Roberto Battistutta ◽  
Stefania Sarno ◽  
Erika De Moliner ◽  
Oriano Marin ◽  
Olaf-G. Issinger ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Protein Kinase ◽  
Protein Kinase Ck2 ◽  
Β Subunit ◽  
Kinase Ck2

Phosphorylation of thymidylate synthase from various sources by human protein kinase CK2 and its catalytic subunits

2010 ◽  
Vol 38 (3) ◽  
pp. 124-131 ◽  
Author(s):  
Tomasz Frączyk ◽  
Konrad Kubiński ◽  
Maciej Masłyk ◽  
Joanna Cieśla ◽  
Ulf Hellman ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Thymidylate Synthase ◽  
Protein Kinase Ck2 ◽  
Human Protein ◽  
Catalytic Subunits ◽  
Human Protein Kinase ◽  
Kinase Ck2

scholarly journals Crystal structures of two furazidin polymorphs revealed by a joint effort of crystal structure prediction and NMR crystallography

2020 ◽  
Vol 76 (3) ◽  
pp. 322-335 ◽  
Author(s):  
Marta K. Dudek ◽  
Piotr Paluch ◽  
Edyta Pindelska
Keyword(s):  
Crystal Structure ◽  
Crystal Structures ◽  
Structure Determination ◽  
Structure Prediction ◽  
Structural Features ◽  
Crystal Structure Determination ◽  
Crystal Structure Prediction ◽  
Crystal Forms ◽  
Space Groups ◽  
Nmr Crystallography

This work presents the crystal structure determination of two elusive polymorphs of furazidin, an antibacterial agent, employing a combination of crystal structure prediction (CSP) calculations and an NMR crystallography approach. Two previously uncharacterized neat crystal forms, one of which has two symmetry-independent molecules (form I), whereas the other one is a Z′ = 1 polymorph (form II), crystallize in P21/c and P 1 space groups, respectively, and both are built by different conformers, displaying different intermolecular interactions. It is demonstrated that the usage of either CSP or NMR crystallography alone is insufficient to successfully elucidate the above-mentioned crystal structures, especially in the case of the Z′ = 2 polymorph. In addition, cases of serendipitous agreement in terms of 1H or 13C NMR data obtained for the CSP-generated crystal structures different from the ones observed in the laboratory (false-positive matches) are analyzed and described. While for the majority of analyzed crystal structures the obtained agreement with the NMR experiment is indicative of some structural features in common with the experimental structure, the mentioned serendipity observed in exceptional cases points to the necessity of caution when using an NMR crystallography approach in crystal structure determination.

Crystal structures of catalytic and regulatory subunits of rat protein kinase CK2

2009 ◽  
Vol 54 (2) ◽  
pp. 220-226 ◽  
Author(s):  
WeiHong Zhou ◽  
XiaoHong Qin ◽  
XiaoJie Yan ◽  
XingQiao Xie ◽  
Liang Li ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Crystal Structures ◽  
Protein Kinase Ck2 ◽  
Regulatory Subunits ◽  
Kinase Ck2

scholarly journals Evidence for Regulation of Mitotic Progression through Temporal Phosphorylation and Dephosphorylation of CK2α

2009 ◽  
Vol 29 (8) ◽  
pp. 2068-2081 ◽  
Author(s):  
Nicole A. St-Denis ◽  
D. Richard Derksen ◽  
David W. Litchfield
Keyword(s):  
Protein Kinase Ck2 ◽  
Spindle Assembly Checkpoint ◽  
Mitotic Catastrophe ◽  
Mitotic Progression ◽  
Proliferating Cells ◽  
Cultured Fibroblasts ◽  
Catalytic Subunits ◽  
Chromosomal Segregation ◽  
Mitotic Phosphorylation ◽  
Kinase Ck2

ABSTRACT Proper mitotic progression is crucial for maintenance of genomic integrity in proliferating cells and is regulated through an intricate series of events, including protein phosphorylation governed by a complex network of protein kinases. One kinase family implicated in the regulation of mitotic progression is protein kinase CK2, a small family of enzymes that is overexpressed in cancer and induces transformation in mice and cultured fibroblasts. CK2α, one isoform of the catalytic subunits of CK2, is maximally phosphorylated at four sites in nocodazole-treated cells. To investigate the effects of CK2α phosphorylation on mitotic progression, we generated phosphospecific antibodies against its mitotic phosphorylation sites. In U2OS cells released from S-phase arrest, these antibodies reveal that CK2α is most highly phosphorylated in prophase and metaphase. Phosphorylation gradually decreases during anaphase and becomes undetectable during telophase and cytokinesis. Stable expression of phosphomimetic CK2α (CK2α-4D, CK2α-4E) results in aberrant centrosome amplification and chromosomal segregation defects and loss of mitotic cells through mitotic catastrophe. Conversely, cells expressing nonphosphorylatable CK2α (CK2α-4A) show a decreased ability to arrest in mitosis following nocodazole treatment, suggesting involvement in the spindle assembly checkpoint. Collectively, these studies indicate that reversible phosphorylation of CK2α requires precise regulation to allow proper mitotic progression.

scholarly journals Specific binding of protein kinase CK2 catalytic subunits to tubulin

FEBS Letters ◽  
1999 ◽  
Vol 462 (1-2) ◽  
pp. 51-56 ◽  
Author(s):  
Michael Faust ◽  
Norbert Schuster ◽  
Mathias Montenarh
Keyword(s):  
Protein Kinase ◽  
Protein Kinase Ck2 ◽  
Specific Binding ◽  
Catalytic Subunits ◽  
Kinase Ck2
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