3BIN: Structure Of The Dal-1 And Tslc1 (372-383) Complex

Perturbed cell adhesion mechanisms are crucial for tumor invasion and metastasis. A cell adhesion protein, TSLC1 (tumor suppressor in lung cancer 1), is inactivated in a majority of metastatic cancers. DAL-1 (differentially expressed in adenocarcinoma of the lung protein), another tumor suppressor, binds through its FERM domain to the TSLC1 C-terminal, 4.1 glycophorin C-like, cytoplasmic domain. However, the molecular basis for this interaction is unknown. Here, we describe the crystal structure of a complex between the DAL-1 FERM domain and a portion of the TSLC1 cytoplasmic domain. DAL-1 binds to TSLC1 through conserved residues in a well defined hydrophobic pocket in the structural C-lobe of the DAL-1 FERM domain. From the crystal structure, it is apparent that Tyr(406) and Thr(408) in the TSLC1 cytoplasmic domain form the most important interactions with DAL-1, and this was also confirmed by surface plasmon resonance studies. Our results refute earlier exon deletion experiments that indicated that glycophorin C interacts with the alpha-lobe of 4.1 FERM domains.
PDB ID: 3BINDownload
MMDB ID: 61884
PDB Deposition Date: 2007/11/30
Updated in MMDB: 2012/09
Experimental Method:
x-ray diffraction
Resolution: 2.3  Å
Source Organism:
synthetic construct
Similar Structures:
Biological Unit for 3BIN: monomeric; determined by author
Molecular Components in 3BIN
Label Count Molecule
Protein (1 molecule)
Band 4.1-like Protein 3(Gene symbol: EPB41L3)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB