3CC0

The Dvl2 PDZ Domain in Complex with the N3 Inhibitory Peptide

Summary for 3CC0

Entry DOI	10.2210/pdb3cc0/pdb
Related	3CBX 3CBY 3CBZ
Descriptor	Dishevelled-2 (2 entities in total)
Functional Keywords	pdz domain, phage derived high affinity ligand, developmental protein, phosphoprotein, wnt signaling pathway, signaling protein, protein binding
Biological source	Homo sapiens (Human)
Cellular location	Cell membrane ; Peripheral membrane protein ; Cytoplasmic side : O14641
Total number of polymer chains	3
Total formula weight	34440.22
Authors	Appleton, B.A.,Wiesmann, C. (deposition date: 2008-02-23, release date: 2009-03-03, Last modification date: 2023-08-30)
Primary citation	Zhang, Y.,Appleton, B.A.,Wiesmann, C.,Lau, T.,Costa, M.,Hannoush, R.N.,Sidhu, S.S. Inhibition of Wnt signaling by Dishevelled PDZ peptides Nat.Chem.Biol., 5:217-219, 2009 Cited by PubMed Abstract: Dishevelled proteins are key regulators of Wnt signaling pathways that have been implicated in the progression of human cancers. We found that the binding cleft of the Dishevelled PDZ domain is more flexible than those of canonical PDZ domains and enables recognition of both C-terminal and internal peptides. These peptide ligands inhibit Wnt/beta-catenin signaling in cells, showing that Dishevelled PDZ domains are potential targets for small-molecule cancer therapeutics. PubMed: 19252499 DOI: 10.1038/nchembio.152 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.75 Å)

Structure validation