PDBsum entry 3e3b

Transferase

PDB id: 3e3b

Contents

Protein chain

334 a.a. *

Ligands

CCK

Waters ×106

* Residue conservation analysis

PDB id:

3e3b

Name:

Transferase

Title:

Crystal structure of catalytic subunit of human protein kinase ck2alpha prime with a potent indazole-derivative inhibitor

Structure:

Casein kinase ii subunit alpha'. Chain: x. Fragment: residues in database 1-334. Synonym: casein kinase ck2 alpha prime, ck ii. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: csnk2a2, ck2a2. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

3.20Å R-factor: 0.268 R-free: 0.274

Authors:

T.Kinoshita,T.Nakaniwa,T.Tada

Key ref:

T.Nakaniwa et al. (2009). Structure of human protein kinase CK2 alpha 2 with a potent indazole-derivative inhibitor. Acta Crystallogr Sect F Struct Biol Cryst Commun, 65, 75-79. PubMed id: 19193990

Date:

07-Aug-08 Release date: 03-Mar-09

Protein chain

P19784  (CSK22_HUMAN) -  Casein kinase II subunit alpha' from Homo sapiens

Seq: 350 a.a.

Struc: 334 a.a.

Enzyme reactions

• Enzyme class: E.C.2.7.11.1 - non-specific serine/threonine protein kinase.
• Reaction:
  1. L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H⁺
  2. L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H⁺

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

Acta Crystallogr Sect F Struct Biol Cryst Commun 65:75-79 (2009)

PubMed id: 19193990

Structure of human protein kinase CK2 alpha 2 with a potent indazole-derivative inhibitor.

T.Nakaniwa, T.Kinoshita, Y.Sekiguchi, T.Tada, I.Nakanishi, K.Kitaura, Y.Suzuki, H.Ohno, A.Hirasawa, G.Tsujimoto.

ABSTRACT

Casein kinase 2 (CK2) is a serine/threonine kinase that functions as a heterotetramer composed of two catalytic subunits (CK2alpha1 or CK2alpha2) and two regulatory subunits (CK2beta). The two isozymes CK2alpha1 and CK2alpha2 play distinguishable roles in healthy subjects and in patients with diseases such as cancer, respectively. In order to develop novel CK2alpha1-selective inhibitors, the crystal structure of human CK2alpha2 (hCK2alpha2) complexed with a potent CK2alpha inhibitor which binds to the active site of hCK2alpha2 was determined and compared with that of human CK2alpha1. While the two isozymes exhibited a high similarity with regard to the active site, the largest structural difference between the isoforms occurred in the beta4-beta5 loop responsible for the CK2alpha-CK2beta interface. The top of the N-terminal segment interacted with the beta4-beta5 loop via a hydrogen bond in hCK2alpha2 but not in hCK2alpha1. Thus, the CK2alpha-CK2beta interface is a likely target candidate for the production of selective CK2alpha1 inhibitors.