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spinqualitylabelsall models 1vzo, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

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