1rqf

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(New page: 200px<br /><applet load="1rqf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rqf, resolution 2.89&Aring;" /> '''Structure of CK2 bet...)
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[[Image:1rqf.gif|left|200px]]<br /><applet load="1rqf" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1rqf.gif|left|200px]]<br /><applet load="1rqf" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1rqf, resolution 2.89&Aring;" />
caption="1rqf, resolution 2.89&Aring;" />
'''Structure of CK2 beta subunit crystallized in the presence of a p21WAF1 peptide'''<br />
'''Structure of CK2 beta subunit crystallized in the presence of a p21WAF1 peptide'''<br />
==Overview==
==Overview==
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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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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==
==About this Structure==
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1RQF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis] with ZN and UNK as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RQF OCA].
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1RQF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=UNK:'>UNK</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQF OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Xenopus laevis]]
[[Category: Xenopus laevis]]
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[[Category: Allende, J.E.]]
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[[Category: Allende, J E.]]
[[Category: Bertrand, L.]]
[[Category: Bertrand, L.]]
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[[Category: Blundell, T.L.]]
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[[Category: Blundell, T L.]]
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[[Category: Bolanos-Garcia, V.M.]]
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[[Category: Bolanos-Garcia, V M.]]
[[Category: Dhanaraj, V.]]
[[Category: Dhanaraj, V.]]
[[Category: Parisini, E.]]
[[Category: Parisini, E.]]
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[[Category: Pei, X.Y.]]
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[[Category: Pei, X Y.]]
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[[Category: Sayed, M.F.]]
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[[Category: Sayed, M F.]]
[[Category: UNK]]
[[Category: UNK]]
[[Category: ZN]]
[[Category: ZN]]
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[[Category: zn finger]]
[[Category: zn finger]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:47:45 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:53:34 2008''

Revision as of 12:53, 21 February 2008


1rqf, resolution 2.89Å

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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

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