1vzo
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(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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Revision as of 19:41, 29 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 [[1]], with EC number [2.7.1.37]. 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
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