1RQF

Structure of CK2 beta subunit crystallized in the presence of a p21WAF1 peptide

Summary for 1RQF

• Entry DOI: 10.2210/pdb1rqf/pdb
• Related: 1JWH 1QF8
• Descriptor: Casein kinase II beta chain, Disordered segment of Cyclin-dependent kinase inhibitor 1, ZINC ION, ... (7 entities in total)
• Functional Keywords: casein kinase beta subunit, ser/thr protein kinase, cyclin-dependent kinase inhibitor, zn finger, transferase
• Biological source: Xenopus laevis (African clawed frog); More
• Total number of polymer chains: 14
• Total formula weight: 173130.25

Authors

Bertrand, L.,Sayed, M.F.,Pei, X.-Y.,Parisini, E.,Dhanaraj, V.,Bolanos-Garcia, V.M.,Allende, J.E.,Blundell, T.L. (deposition date: 2003-12-05, release date: 2004-10-05, Last modification date: 2023-08-23)

Primary citation

Bertrand, L.,Sayed, M.F.,Pei, X.Y.,Parisini, E.,Dhanaraj, V.,Bolanos-Garcia, V.M.,Allende, J.E.,Blundell, T.L.
Structure of the regulatory subunit of CK2 in the presence of a p21WAF1 peptide demonstrates flexibility of the acidic loop.
Acta Crystallogr.,Sect.D, 60:1698-1704, 2004

PubMed Abstract: 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.

PubMed: 15388915
DOI: 10.1107/S0907444904016750

Experimental method

X-RAY DIFFRACTION (2.89 Å)