|
|
| Line 1: |
Line 1: |
| [[Image:1upl.jpg|left|200px]] | | {{Seed}} |
| | [[Image:1upl.png|left|200px]] |
|
| |
|
| <!-- | | <!-- |
| Line 9: |
Line 10: |
| {{STRUCTURE_1upl| PDB=1upl | SCENE= }} | | {{STRUCTURE_1upl| PDB=1upl | SCENE= }} |
|
| |
|
| '''CRYSTAL STRUCTURE OF MO25 ALPHA'''
| | ===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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_14730349}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 14730349 is the PubMed ID number. |
| | --> |
| | {{ABSTRACT_PUBMED_14730349}} |
|
| |
|
| ==About this Structure== | | ==About this Structure== |
| Line 31: |
Line 35: |
| [[Category: Mo25]] | | [[Category: Mo25]] |
| [[Category: Strad]] | | [[Category: Strad]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:32:21 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:28:49 2008'' |