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1vzo

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[[Image:1vzo.gif|left|200px]]<br /><applet load="1vzo" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1vzo.gif|left|200px]]
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caption="1vzo, resolution 1.80&Aring;" />
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'''THE STRUCTURE OF THE N-TERMINAL KINASE DOMAIN OF MSK1 REVEALS A NOVEL AUTOINHIBITORY CONFORMATION FOR A DUAL KINASE PROTEIN'''<br />
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{{Structure
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|PDB= 1vzo |SIZE=350|CAPTION= <scene name='initialview01'>1vzo</scene>, resolution 1.80&Aring;
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|SITE= <scene name='pdbsite=BME:So4+Binding+Site+For+Chain+A'>BME</scene>
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Transferred_entry:_2.7.11.1 Transferred entry: 2.7.11.1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.37 2.7.1.37]
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|GENE=
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}}
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'''THE STRUCTURE OF THE N-TERMINAL KINASE DOMAIN OF MSK1 REVEALS A NOVEL AUTOINHIBITORY CONFORMATION FOR A DUAL KINASE PROTEIN'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1VZO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=BME:'>BME</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Transferred_entry:_2.7.11.1 Transferred entry: 2.7.11.1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.37 2.7.1.37] Known structural/functional Site: <scene name='pdbsite=BME:So4+Binding+Site+For+Chain+A'>BME</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VZO OCA].
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1VZO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VZO OCA].
==Reference==
==Reference==
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The structure of MSK1 reveals a novel autoinhibitory conformation for a dual kinase protein., Smith KJ, Carter PS, Bridges A, Horrocks P, Lewis C, Pettman G, Clarke A, Brown M, Hughes J, Wilkinson M, Bax B, Reith A, Structure. 2004 Jun;12(6):1067-77. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15274926 15274926]
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The structure of MSK1 reveals a novel autoinhibitory conformation for a dual kinase protein., Smith KJ, Carter PS, Bridges A, Horrocks P, Lewis C, Pettman G, Clarke A, Brown M, Hughes J, Wilkinson M, Bax B, Reith A, Structure. 2004 Jun;12(6):1067-77. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15274926 15274926]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:39:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:50:11 2008''

Revision as of 12:50, 20 March 2008

Image:1vzo.gif


PDB ID 1vzo

Drag the structure with the mouse to rotate
, resolution 1.80Å
Sites:
Ligands: and
Activity: Transferred entry: 2.7.11.1, with EC number 2.7.1.37
Coordinates: save as pdb, mmCIF, xml



THE STRUCTURE OF THE N-TERMINAL KINASE DOMAIN OF MSK1 REVEALS A NOVEL AUTOINHIBITORY CONFORMATION FOR A DUAL KINASE PROTEIN


Contents

Overview

Mitogen and stress-activated kinase-1 (MSK1) is a serine/threonine protein kinase that is activated by either p38 or p42ERK MAPKs in response to stress or mitogenic extracellular stimuli. MSK1 belongs to a family of protein kinases that contain two distinct kinase domains in one polypeptide chain. We report the 1.8 A crystal structure of the N-terminal kinase domain of MSK1. The crystal structure reveals a unique inactive conformation with the ATP binding site blocked by the nucleotide binding loop. This inactive conformation is stabilized by the formation of a new three-stranded beta sheet on the N lobe of the kinase domain. The three beta strands come from residues at the N terminus of the kinase domain, what would be the alphaB helix in the active conformation, and the activation loop. The new three-stranded beta sheet occupies a position equivalent to the N terminus of the alphaC helix in active protein kinases.

Disease

Known disease associated with this structure: Spondyloepiphyseal dysplasia, Kimberley type OMIM:[155760]

About this Structure

1VZO is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The structure of MSK1 reveals a novel autoinhibitory conformation for a dual kinase protein., Smith KJ, Carter PS, Bridges A, Horrocks P, Lewis C, Pettman G, Clarke A, Brown M, Hughes J, Wilkinson M, Bax B, Reith A, Structure. 2004 Jun;12(6):1067-77. PMID:15274926

Page seeded by OCA on Thu Mar 20 14:50:11 2008

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