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1upk
From Proteopedia
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|PDB= 1upk |SIZE=350|CAPTION= <scene name='initialview01'>1upk</scene>, resolution 1.85Å | |PDB= 1upk |SIZE=350|CAPTION= <scene name='initialview01'>1upk</scene>, resolution 1.85Å | ||
|SITE= <scene name='pdbsite=AC1:Mes+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Mes+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC ACID'>MES</scene> | + | |LIGAND= <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1upk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1upk OCA], [http://www.ebi.ac.uk/pdbsum/1upk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1upk RCSB]</span> | ||
}} | }} | ||
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[[Category: Deak, M.]] | [[Category: Deak, M.]] | ||
[[Category: Milburn, C C.]] | [[Category: Milburn, C C.]] | ||
| - | [[Category: MES]] | ||
[[Category: armadillo]] | [[Category: armadillo]] | ||
[[Category: mo25]] | [[Category: mo25]] | ||
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[[Category: strad]] | [[Category: strad]] | ||
| - | ''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 00:13:36 2008'' |
Revision as of 21:13, 30 March 2008
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| , resolution 1.85Å | |||||||
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| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF MO25 IN COMPLEX WITH A C-TERMINAL PEPTIDE OF STRAD
Overview
Mouse protein 25 alpha (MO25 alpha) is a 40-kDa protein that, together with the STE20-related adaptor-alpha (STRAD alpha) pseudo kinase, forms a regulatory complex capable of stimulating the activity of the LKB1 tumor suppressor protein kinase. The latter is mutated in the inherited Peutz-Jeghers cancer syndrome (PJS). MO25 alpha binds directly to a conserved Trp-Glu-Phe sequence at the STRAD alpha C terminus, markedly enhancing binding of STRAD alpha to LKB1 and increasing LKB1 catalytic activity. The MO25 alpha crystal structure reveals a helical repeat fold, distantly related to the Armadillo proteins. A complex with the STRAD alpha peptide reveals a hydrophobic pocket that is involved in a unique and specific interaction with the Trp-Glu-Phe motif, further supported by mutagenesis studies. The data represent a first step toward structural analysis of the LKB1-STRAD-MO25 complex, and suggests that MO25 alpha is a scaffold protein to which other regions of STRAD-LKB1, cellular LKB1 substrates or regulatory components could bind.
About this Structure
1UPK is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of MO25 alpha in complex with the C terminus of the pseudo kinase STE20-related adaptor., Milburn CC, Boudeau J, Deak M, Alessi DR, van Aalten DM, Nat Struct Mol Biol. 2004 Feb;11(2):193-200. Epub 2004 Jan 18. PMID:14730349
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