http://purl.uniprot.org/citations/21131357 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/21131357 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/21131357 | http://www.w3.org/2000/01/rdf-schema#comment | "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."xsd:string |
http://purl.uniprot.org/citations/21131357 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m110.174011"xsd:string |
http://purl.uniprot.org/citations/21131357 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m110.174011"xsd:string |
http://purl.uniprot.org/citations/21131357 | http://purl.uniprot.org/core/author | "Persson C."xsd:string |
http://purl.uniprot.org/citations/21131357 | http://purl.uniprot.org/core/author | "Persson C."xsd:string |
http://purl.uniprot.org/citations/21131357 | http://purl.uniprot.org/core/author | "Flores A."xsd:string |
http://purl.uniprot.org/citations/21131357 | http://purl.uniprot.org/core/author | "Flores A."xsd:string |
http://purl.uniprot.org/citations/21131357 | http://purl.uniprot.org/core/author | "Hammarstrom M."xsd:string |
http://purl.uniprot.org/citations/21131357 | http://purl.uniprot.org/core/author | "Hammarstrom M."xsd:string |
http://purl.uniprot.org/citations/21131357 | http://purl.uniprot.org/core/author | "Thorsell A.G."xsd:string |
http://purl.uniprot.org/citations/21131357 | http://purl.uniprot.org/core/author | "Thorsell A.G."xsd:string |
http://purl.uniprot.org/citations/21131357 | http://purl.uniprot.org/core/author | "Busam R.D."xsd:string |
http://purl.uniprot.org/citations/21131357 | http://purl.uniprot.org/core/author | "Busam R.D."xsd:string |
http://purl.uniprot.org/citations/21131357 | http://purl.uniprot.org/core/author | "Hallberg B.M."xsd:string |
http://purl.uniprot.org/citations/21131357 | http://purl.uniprot.org/core/author | "Hallberg B.M."xsd:string |
http://purl.uniprot.org/citations/21131357 | http://purl.uniprot.org/core/author | "Obrink B."xsd:string |
http://purl.uniprot.org/citations/21131357 | http://purl.uniprot.org/core/author | "Obrink B."xsd:string |
http://purl.uniprot.org/citations/21131357 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
http://purl.uniprot.org/citations/21131357 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
http://purl.uniprot.org/citations/21131357 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/21131357 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/21131357 | http://purl.uniprot.org/core/pages | "4511-4516"xsd:string |
http://purl.uniprot.org/citations/21131357 | http://purl.uniprot.org/core/pages | "4511-4516"xsd:string |