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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 60 1698-704 (2004)
Cited: 2 times
EuropePMC logo PMID: 15388915

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.

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  1. Positioning of proteins in membranes: a computational approach. Lomize AL, Pogozheva ID, Lomize MA, Mosberg HI. Protein Sci 15 1318-1333 (2006)


Reviews citing this publication (1)

  1. Cellular regulators of protein kinase CK2. Montenarh M. Cell Tissue Res 342 139-146 (2010)


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