1vzo
From Proteopedia
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|PDB= 1vzo |SIZE=350|CAPTION= <scene name='initialview01'>1vzo</scene>, resolution 1.80Å | |PDB= 1vzo |SIZE=350|CAPTION= <scene name='initialview01'>1vzo</scene>, resolution 1.80Å | ||
|SITE= <scene name='pdbsite=BME:So4+Binding+Site+For+Chain+A'>BME</scene> | |SITE= <scene name='pdbsite=BME:So4+Binding+Site+For+Chain+A'>BME</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/ | + | |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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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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==Overview== | ==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. | 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. | ||
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| - | ==Disease== | ||
| - | Known disease associated with this structure: Spondyloepiphyseal dysplasia, Kimberley type OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=155760 155760]] | ||
==About this Structure== | ==About this Structure== | ||
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15274926 15274926] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15274926 15274926] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| + | [[Category: Non-specific serine/threonine protein kinase]] | ||
[[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: Smith, K J.]] | [[Category: Smith, K J.]] | ||
[[Category: Wilkinson, M.]] | [[Category: Wilkinson, M.]] | ||
| - | [[Category: BME]] | ||
| - | [[Category: SO4]] | ||
[[Category: phosphorylation]] | [[Category: phosphorylation]] | ||
[[Category: protein kinase]] | [[Category: protein kinase]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:29:11 2008'' |
Revision as of 21:29, 30 March 2008
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| , resolution 1.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Activity: | Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Mon Mar 31 00:29:11 2008
Categories: Homo sapiens | Non-specific serine/threonine protein kinase | Single protein | 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. | Phosphorylation | Protein kinase | Serine/threonine protein kinase | Transferase
