1day | pdb_00001day

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Revision as of 11:00, 20 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1day" size="450" color="white" frame="true" align="right" spinBox="true" caption="1day, resolution 2.2Å" /> '''CRYSTAL STRUCTURE OF ...)
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File:1day.jpg


1day, resolution 2.2Å

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CRYSTAL STRUCTURE OF A BINARY COMPLEX OF PROTEIN KINASE CK2 (ALPHA-SUBUNIT) AND MG-GMPPNP

Overview

The structures of the catalytic subunit of protein kinase CK2 from Zea, mays complexed with Mg2+ and with analogs of ATP or GTP were determined to, 2.2 A resolution. Unlike most other protein kinases, CK2 from various, sources shows 'dual-cosubstrate specificity', that is, the ability to, efficiently use either ATP or GTP as a cosubstrate. The structures of, these complexes demonstrate that water molecules are critical to switch, the active site of CK2 from an ATP- to a GTP-compatible state. An, understanding of the structural basis of dual-cosubstrate specificity may, help in the design of drugs that target CK2 or other kinases with this, property.

About this Structure

1DAY is a Single protein structure of sequence from Zea mays with MG and GNP 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

GTP plus water mimic ATP in the active site of protein kinase CK2., Niefind K, Putter M, Guerra B, Issinger OG, Schomburg D, Nat Struct Biol. 1999 Dec;6(12):1100-3. PMID:10581548

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