1rqf
From Proteopedia
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Structure of CK2 beta subunit crystallized in the presence of a p21WAF1 peptide
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 with and as ligands. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 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 Feb 21 14:53:34 2008
Categories: Non-specific serine/threonine protein kinase | Single protein | Xenopus laevis | Allende, J E. | Bertrand, L. | Blundell, T L. | Bolanos-Garcia, V M. | Dhanaraj, V. | Parisini, E. | Pei, X Y. | Sayed, M F. | UNK | ZN | Casein kinase beta subunit | Cyclin-dependent kinase inhibitor | Ser/thr protein kinase | Zn finger
