3BIN

Structure of the DAL-1 and TSLC1 (372-383) complex

Summary for 3BIN

• Entry DOI: 10.2210/pdb3bin/pdb
• Related: 2HE7
• Descriptor: Band 4.1-like protein 3, Cell adhesion molecule 1 (3 entities in total)
• Functional Keywords: ferm domain, dal-1, tslc1, actin-binding, cytoskeleton, phosphoprotein, structural protein, anti-oncogene, apoptosis, cell adhesion, cell cycle, developmental protein, differentiation, glycoprotein, immune response, immunoglobulin domain, membrane, spermatogenesis, transmembrane
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm, cytoskeleton (By similarity): Q9Y2J2; Cell membrane; Single-pass type I membrane protein: Q9BY67
• Total number of polymer chains: 2
• Total formula weight: 34443.37

Authors

Busam, R.D.,Arrowsmith, C.H.,Collins, R.,Dahlgren, L.G.,Edwards, A.M.,Flodin, S.,Flores, A.,Graslund, S.,Hammarstrom, M.,Johansson, A.,Johansson, I.,Kallas, A.,Karlberg, T.,Kotenyova, T.,Lehtio, L.,Moche, M.,Nilsson, M.E.,Nordlund, P.,Nyman, T.,Sagemark, J.,Svensson, L.,Thorsell, A.G.,Tresaugues, L.,Van Den Berg, S.,Weigelt, J.,Welin, M.,Berglund, H.,Persson, C.,Hallberg, B.M. (deposition date: 2007-11-30, release date: 2008-01-15, Last modification date: 2024-03-13)

Primary citation

Busam, R.D.,Thorsell, A.-G.,Flores, A.,Hammarstrom, M.,Persson, C.,Obrink, B.,Hallberg, B.M.
Structural basis of tumor suppressor in lung cancer 1 (TSLC1) binding to differentially expressed in adenocarcinoma of the lung (DAL-1/4.1B)
J.Biol.Chem., 286:4511-4516, 2011

PubMed Abstract: 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 α-lobe of 4.1 FERM domains.

PubMed: 21131357
DOI: 10.1074/jbc.M110.174011

Experimental method

X-RAY DIFFRACTION (2.3 Å)