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The structure of MSK1 reveals a novel autoinhibitory conformation for a dual kinase protein

Smith, Kathrine J, Carter, Paul S, Bridges, Angela, Horrocks, Pete, Lewis, Ceri, Pettman, Gary, Clarke, Andrew, Brown, Murray, Hughes, Jane, Wilkinson, Marc, Bax, Benjamin and Reith, Alastair 2004. The structure of MSK1 reveals a novel autoinhibitory conformation for a dual kinase protein. Structure 12 (6) , pp. 1067-1077. 10.1016/j.str.2004.02.040

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Abstract

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 Å 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 β sheet on the N lobe of the kinase domain. The three β strands come from residues at the N terminus of the kinase domain, what would be the αB helix in the active conformation, and the activation loop. The new three-stranded β sheet occupies a position equivalent to the N terminus of the αC helix in active protein kinases.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Biosciences
Publisher: Elsevier (Cell Press)
ISSN: 0969-2126
Date of Acceptance: 12 February 2004
Last Modified: 18 Jul 2018 13:31
URI: http://orca.cardiff.ac.uk/id/eprint/112633

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