1fsh
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STRUCTURAL BASIS OF THE RECOGNITION OF THE DISHEVELLED DEP DOMAIN IN THE WNT SIGNALING PATHWAY
OverviewOverview
The DEP domain of Dishevelled (Dvl) proteins transduces signals to, effector proteins downstream of Dvl in the Wnt pathway. Here we report, that DEP-containing mutants inhibit Wnt-induced, but not Dvl-induced, activation of the transcription factor Lef-1. This inhibitory effect is, weakened by a K434M mutation. Nuclear magnetic resonance spectroscopy, revealed that the DEP domain of mouse Dvl1 comprises a three-helix bundle, a beta-hairpin 'arm' and two short beta-strands at the C-terminal region., Lys 434 is located at the tip of the beta-hairpin 'arm'. Based on our, findings, we conclude that DEP interacts with regulators upstream of Dvl, via a strong electric dipole on the molecule's surface created by Lys 434, Asp 445 and Asp 448; the electric dipole and the putative membrane binding, site are at two different locations.
About this StructureAbout this Structure
1FSH is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis of the recognition of the dishevelled DEP domain in the Wnt signaling pathway., Wong HC, Mao J, Nguyen JT, Srinivas S, Zhang W, Liu B, Li L, Wu D, Zheng J, Nat Struct Biol. 2000 Dec;7(12):1178-84. PMID:11101902
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