1FSH
STRUCTURAL BASIS OF THE RECOGNITION OF THE DISHEVELLED DEP DOMAIN IN THE WNT SIGNALING PATHWAY
Summary for 1FSH
| Entry DOI | 10.2210/pdb1fsh/pdb |
| Descriptor | DISHEVELLED-1 (1 entity in total) |
| Functional Keywords | three-helix bundle, beta-arm, dishevelled-1, segment polarity protein dishevelled homolog dvl-1, signaling protein |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 11934.70 |
| Authors | Wong, H.C.,Zheng, J. (deposition date: 2000-09-08, release date: 2001-03-08, Last modification date: 2024-05-29) |
| Primary citation | Wong, H.C.,Mao, J.,Nguyen, J.T.,Srinivas, S.,Zhang, W.,Liu, B.,Li, L.,Wu, D.,Zheng, J. Structural basis of the recognition of the dishevelled DEP domain in the Wnt signaling pathway. Nat.Struct.Biol., 7:1178-1184, 2000 Cited by PubMed Abstract: 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. PubMed: 11101902DOI: 10.1038/82047 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
