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1vzo
From Proteopedia
(New page: 200px<br /> <applet load="1vzo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vzo, resolution 1.80Å" /> '''THE STRUCTURE OF TH...) |
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==About this Structure== | ==About this Structure== | ||
| - | 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 SO4 and BME as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.37 2.7.1.37]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VZO OCA]]. | + | 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 SO4 and BME 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]]. Structure known Active Site: BME. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VZO OCA]]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| + | [[Category: Transferred entry: 2.7.11.1]] | ||
[[Category: Bax, B.]] | [[Category: Bax, B.]] | ||
[[Category: Bridges, A.]] | [[Category: Bridges, A.]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:15:25 2007'' |
Revision as of 12:10, 30 October 2007
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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, ... [(full description)]
About this Structure
1VZO is a [Single protein] structure of sequence from [Homo sapiens] with SO4 and BME as [ligands]. Active as [Transferred entry: 2.7.11.1], with EC number [2.7.1.37]. Structure known Active Site: BME. 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 Tue Oct 30 14:15:25 2007
Categories: Homo sapiens | Single protein | Transferred entry: 2.7.11.1 | Bax, B. | Bridges, A. | Brown, M. | Carter, P.S. | Clarke, A. | Horrocks, P. | Hughes, J. | Lewis, C. | Pettman, G. | Reith, A. | Smith, K.J. | Wilkinson, M. | BME | SO4 | Phosphorylation | Protein kinase | Serine/threonine protein kinase | Transferase
