Structure of the regulatory subunit of CK2 in the presence of a p21WAF1 peptide demonstrates flexibility of the acidic loop

被引:7
作者
Bertrand, L
Sayed, MFR
Pei, XY
Parisini, E
Dhanaraj, V
Bolanos-Garcia, VM
Allende, JE
Blundell, TL
机构
[1] Univ Cambridge, Dept Biochem, Cambridge CB2 1GA, England
[2] Univ Chile, Fac Med, ICBM, Programa Biol Celular & Mol, Santiago 7, Chile
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2004年 / 60卷
关键词
D O I
10.1107/S0907444904016750
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
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 p21(WAF1) ( residues 46 - 65) and the structure solved at 2.9 Angstrom 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 p21(WAF1). This binding site corresponds to the solvent-accessible part of the conserved zinc-finger motif.
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页码:1698 / 1704
页数:7
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