NMR structure of the mDvl1 PDZ domain in complex with its inhibitor
The structure was published by Lee, H.J., Wang, N.X., Shi, D.L., and Zheng, J.J., in 2009 in a paper entitled "Sulindac inhibits canonical Wnt signaling by blocking the PDZ domain of the protein Dishevelled." (abstract).
The structure was determined using NMR spectroscopy and deposited in 2008.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of Segment polarity protein dishevelled homolog DVL-1. This molecule has the UniProt identifier P51141 (DVL1_MOUSE). The sample contained 90 residues which is < 90% of the natural sequence. Out of 90 residues 90 were observed and are deposited in the PDB.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
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: