2HE7

FERM domain of EPB41L3 (DAL-1)

Summary for 2HE7

• Entry DOI: 10.2210/pdb2he7/pdb
• Descriptor: Band 4.1-like protein 3 (2 entities in total)
• Functional Keywords: ferm domain, dal-1, epb41l3a, structural genomics, structural genomics consortium, sgc, cell adhesion
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytoskeleton (By similarity): Q9Y2J2
• Total number of polymer chains: 1
• Total formula weight: 33079.92

Authors

Hallberg, B.M.,Busam, R.D.,Arrowsmith, C.,Berglund, H.,Collins, R.,Edwards, A.,Ehn, M.,Flodin, S.,Flores, A.,Graslund, S.,Hammarstrom, M.,Schiavone, L.H.,Johansson, I.,Hogbom, M.,Karlberg, T.,Kotenyova, T.,Nilvebrandt, J.,Norberg, P.,Stenmark, P.,Nordlund, P.,Nilsson-ehle, P.,Nyman, T.,Ogg, D.,Sagemark, J.,Sundstrom, M.,Uppenberg, J.,Van den berg, S.,Weigelt, J.,Persson, C.,Thorsell, A.G.,Structural Genomics Consortium (SGC) (deposition date: 2006-06-21, release date: 2006-07-04, Last modification date: 2024-02-14)

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 Å)