1rqf | pdb_00001rqf
Structure of CK2 beta subunit crystallized in the presence of a p21WAF1 peptide
| |||||||||||||
| 1rqf, resolution 2.89Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | ZN and UNK | ||||||||||||
| Gene: | KC2B (Xenopus laevis) | ||||||||||||
| Activity: | Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Overview
A truncated form of the regulatory subunit of the protein kinase CK2beta (residues 1-178) has been crystallized in the presence of a fragment of the cyclin-dependent kinase inhibitor p21WAF1 (residues 46-65) and the structure solved at 2.9 A resolution by molecular replacement. The core of the CK2beta dimer shows a high structural similarity with that identified in previous structural analyses of the dimer and the holoenzyme. However, the electron density corresponding to the substrate-binding acidic loop (residues 55-64) indicates two conformations that differ from that of the holoenzyme structure [Niefind et al. (2001), EMBO J. 20, 5320-5331]. Difference electron density near the dimerization region in each of the eight protomers in the asymmetric unit is attributed to between one and eight amino-acid residues of a complexed fragment of p21WAF1. This binding site corresponds to the solvent-accessible part of the conserved zinc-finger motif.
About this Structure
1RQF is a Single protein structure of sequence from Xenopus laevis. Full crystallographic information is available from OCA.
Reference
Structure of the regulatory subunit of CK2 in the presence of a p21WAF1 peptide demonstrates flexibility of the acidic loop., Bertrand L, Sayed MF, Pei XY, Parisini E, Dhanaraj V, Bolanos-Garcia VM, Allende JE, Blundell TL, Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1698-704. Epub, 2004 Sep 23. PMID:15388915
Page seeded by OCA on Thu Mar 20 13:54:56 2008
