This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1rqf

From Proteopedia

Revision as of 20:31, 30 March 2008 by OCA (Talk | contribs)
Jump to: navigation, search


PDB ID 1rqf

Drag the structure with the mouse to rotate
, resolution 2.89Å
Ligands: ,
Gene: KC2B (Xenopus laevis)
Activity: Non-specific serine/threonine protein kinase, with EC number 2.7.11.1
Related: 1QF8, 1JWH


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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. 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 Sun Mar 30 23:31:36 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools