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1upl

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==Overview==
==Overview==
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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.
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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==
==About this Structure==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Aalten, D.M.F.Van.]]
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[[Category: Aalten, D M.F Van.]]
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[[Category: Alessi, D.R.]]
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[[Category: Alessi, D R.]]
[[Category: Boudeau, J.]]
[[Category: Boudeau, J.]]
[[Category: Deak, M.]]
[[Category: Deak, M.]]
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[[Category: Milburn, C.C.]]
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[[Category: Milburn, C C.]]
[[Category: armadillo]]
[[Category: armadillo]]
[[Category: lkb1]]
[[Category: lkb1]]
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[[Category: strad]]
[[Category: strad]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:03:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:27:06 2008''

Revision as of 13:27, 21 February 2008


1upl, resolution 2.60Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF MO25 ALPHA

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

1UPL is a Single protein structure of sequence 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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