STRUCTURAL BASIS OF THE RECOGNITION OF THE DISHEVELLED DEP DOMAIN IN THE WNT SIGNALING PATHWAY
The structure was published by Wong, H.C., Mao, J., Nguyen, J.T., et al., Li, L., Wu, D., and Zheng, J., in 2000 in a paper entitled "Structural basis of the recognition of the dishevelled DEP domain in the Wnt signaling pathway." (abstract).
The structure was determined using NMR spectroscopy and deposited in 2000.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of DISHEVELLED-1. This molecule has the UniProt identifier P51141 (DVL1_MOUSE). The sample contained 105 residues which is < 90% of the natural sequence. Out of 105 residues 94 were observed and are deposited in the PDB.
The molecule is most likely monomeric.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 1 unique UniProt protein: