1f0q

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1f0q.jpg|left|200px]]<br /><applet load="1f0q" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1f0q.jpg|left|200px]]
-
caption="1f0q, resolution 2.63&Aring;" />
+
 
-
'''CRYSTAL STRUCTURE OF THE ALPHA SUBUNIT OF PROTEIN KINASE CK2 IN COMPLEX WITH THE NUCLEOTIDE COMPETITIVE INHIBITOR EMODIN'''<br />
+
{{Structure
 +
|PDB= 1f0q |SIZE=350|CAPTION= <scene name='initialview01'>1f0q</scene>, resolution 2.63&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=EMO:3-METHYL-1,6,8-TRIHYDROXYANTHRAQUINONE'>EMO</scene>
 +
|ACTIVITY= [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]
 +
|GENE=
 +
}}
 +
 
 +
'''CRYSTAL STRUCTURE OF THE ALPHA SUBUNIT OF PROTEIN KINASE CK2 IN COMPLEX WITH THE NUCLEOTIDE COMPETITIVE INHIBITOR EMODIN'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1F0Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays] with <scene name='pdbligand=EMO:'>EMO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1F0Q OCA].
+
1F0Q is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F0Q OCA].
==Reference==
==Reference==
-
The replacement of ATP by the competitive inhibitor emodin induces conformational modifications in the catalytic site of protein kinase CK2., Battistutta R, Sarno S, De Moliner E, Papinutto E, Zanotti G, Pinna LA, J Biol Chem. 2000 Sep 22;275(38):29618-22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10882732 10882732]
+
The replacement of ATP by the competitive inhibitor emodin induces conformational modifications in the catalytic site of protein kinase CK2., Battistutta R, Sarno S, De Moliner E, Papinutto E, Zanotti G, Pinna LA, J Biol Chem. 2000 Sep 22;275(38):29618-22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10882732 10882732]
[[Category: Non-specific serine/threonine protein kinase]]
[[Category: Non-specific serine/threonine protein kinase]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 23: Line 32:
[[Category: protein kinase-inhibitor complex]]
[[Category: protein kinase-inhibitor complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:33:35 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:02:52 2008''

Revision as of 09:02, 20 March 2008


PDB ID 1f0q

Drag the structure with the mouse to rotate
, resolution 2.63Å
Ligands:
Activity: Non-specific serine/threonine protein kinase, with EC number 2.7.11.1
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF THE ALPHA SUBUNIT OF PROTEIN KINASE CK2 IN COMPLEX WITH THE NUCLEOTIDE COMPETITIVE INHIBITOR EMODIN


Overview

The structure of a complex between the catalytic subunit of Zea mays CK2 and the nucleotide binding site-directed inhibitor emodin (3-methyl-1,6,8-trihydroxyanthraquinone) was solved at 2.6-A resolution. Emodin enters the nucleotide binding site of the enzyme, filling a hydrophobic pocket between the N-terminal and the C-terminal lobes, in the proximity of the site occupied by the base rings of the natural co-substrates. The interactions between the inhibitor and CK2 alpha are mainly hydrophobic. Although the C-terminal domain of the enzyme is essentially identical to the ATP-bound form, the beta-sheet in the N-terminal domain is altered by the presence of emodin. The structural data presented here highlight the flexibility of the kinase domain structure and provide information for the design of selective ATP competitive inhibitors of protein kinase CK2.

About this Structure

1F0Q is a Single protein structure of sequence from Zea mays. Full crystallographic information is available from OCA.

Reference

The replacement of ATP by the competitive inhibitor emodin induces conformational modifications in the catalytic site of protein kinase CK2., Battistutta R, Sarno S, De Moliner E, Papinutto E, Zanotti G, Pinna LA, J Biol Chem. 2000 Sep 22;275(38):29618-22. PMID:10882732

Page seeded by OCA on Thu Mar 20 11:02:52 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools