1pjk
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1pjk.jpg|left|200px]] | + | [[Image:1pjk.jpg|left|200px]] |
| - | + | ||
| - | '''Crystal Structure of a C-terminal deletion mutant of human protein kinase CK2 catalytic subunit''' | + | {{Structure |
| + | |PDB= 1pjk |SIZE=350|CAPTION= <scene name='initialview01'>1pjk</scene>, resolution 2.50Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER'>ANP</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] | ||
| + | |GENE= CSNK2A1 OR CK2A1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure of a C-terminal deletion mutant of human protein kinase CK2 catalytic subunit''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1PJK is a [ | + | 1PJK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PJK OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of a C-terminal deletion mutant of human protein kinase CK2 catalytic subunit., Ermakova I, Boldyreff B, Issinger OG, Niefind K, J Mol Biol. 2003 Jul 25;330(5):925-34. PMID:[http:// | + | Crystal structure of a C-terminal deletion mutant of human protein kinase CK2 catalytic subunit., Ermakova I, Boldyreff B, Issinger OG, Niefind K, J Mol Biol. 2003 Jul 25;330(5):925-34. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12860116 12860116] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Non-specific serine/threonine protein kinase]] | [[Category: Non-specific serine/threonine protein kinase]] | ||
| Line 22: | Line 31: | ||
[[Category: eukaryotic protein kinase fold]] | [[Category: eukaryotic protein kinase fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:25:13 2008'' |
Revision as of 11:25, 20 March 2008
| |||||||
| , resolution 2.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | CSNK2A1 OR CK2A1 (Homo sapiens) | ||||||
| Activity: | Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of a C-terminal deletion mutant of human protein kinase CK2 catalytic subunit
Overview
Protein kinase CK2 (formerly called: casein kinase 2) is a heterotetrameric enzyme composed of two separate catalytic chains (CK2alpha) and a stable dimer of two non-catalytic subunits (CK2beta). CK2alpha is a highly conserved member of the superfamily of eukaryotic protein kinases. The crystal structure of a C-terminal deletion mutant of human CK2alpha was solved and refined to 2.5A resolution. In the crystal the CK2alpha mutant exists as a monomer in agreement with the organization of the subunits in the CK2 holoenzyme. The refined structure shows the helix alphaC and the activation segment, two main regions of conformational plasticity and regulatory importance in eukaryotic protein kinases, in active conformations stabilized by extensive contacts to the N-terminal segment. This arrangement is in accordance with the constitutive activity of the enzyme. By structural superimposition of human CK2alpha in isolated form and embedded in the human CK2 holoenzyme the loop connecting the strands beta4 and beta5 and the ATP-binding loop were identified as elements of structural variability. This structural comparison suggests that the ATP-binding loop may be the key region by which the non-catalytic CK2beta dimer modulates the activity of CK2alpha. The beta4/beta5 loop was found in a closed conformation in contrast to the open conformation observed for the CK2alpha subunits of the CK2 holoenzyme. CK2alpha monomers with this closed beta4/beta5 loop conformation are unable to bind CK2beta dimers in the common way for sterical reasons, suggesting a mechanism to protect CK2alpha from integration into CK2 holoenzyme complexes. This observation is consistent with the growing evidence that CK2alpha monomers and CK2beta dimers can exist in vivo independently from the CK2 holoenzyme and may possess physiological roles of their own.
About this Structure
1PJK is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of a C-terminal deletion mutant of human protein kinase CK2 catalytic subunit., Ermakova I, Boldyreff B, Issinger OG, Niefind K, J Mol Biol. 2003 Jul 25;330(5):925-34. PMID:12860116
Page seeded by OCA on Thu Mar 20 13:25:13 2008
