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[[Image:1vzo.gif|left|200px]]
[[Image:1vzo.gif|left|200px]]


{{Structure
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|SITE= <scene name='pdbsite=BME:So4+Binding+Site+For+Chain+A'>BME</scene>
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vzo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vzo OCA], [http://www.ebi.ac.uk/pdbsum/1vzo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vzo RCSB]</span>
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'''THE STRUCTURE OF THE N-TERMINAL KINASE DOMAIN OF MSK1 REVEALS A NOVEL AUTOINHIBITORY CONFORMATION FOR A DUAL KINASE PROTEIN'''
'''THE STRUCTURE OF THE N-TERMINAL KINASE DOMAIN OF MSK1 REVEALS A NOVEL AUTOINHIBITORY CONFORMATION FOR A DUAL KINASE PROTEIN'''
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[[Category: Smith, K J.]]
[[Category: Smith, K J.]]
[[Category: Wilkinson, M.]]
[[Category: Wilkinson, M.]]
[[Category: phosphorylation]]
[[Category: Phosphorylation]]
[[Category: protein kinase]]
[[Category: Protein kinase]]
[[Category: serine/threonine protein kinase]]
[[Category: Serine/threonine protein kinase]]
[[Category: transferase]]
[[Category: Transferase]]
 
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Revision as of 09:57, 3 May 2008

File:1vzo.gif

Template:STRUCTURE 1vzo

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


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.

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 Sat May 3 12:57:35 2008

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