2he7

FERM domain of EPB41L3 (DAL-1)

spinqualitylabelsall models 2he7, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2he7 is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: EPB41L3 (HUMAN) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [E41L3_HUMAN] Critical growth regulator in the pathogenesis of meningiomas. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Perturbed cell-adhesion mechanisms are crucial for tumor invasion and metastasis. A cell-adhesion protein, Tumor Suppressor in Lung Cancer 1 (TSLC1), 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 DAL-1 FERM domain's structural C-lobe. From the crystal structure, it is apparent that Tyr406 and Thr408 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. Structural basis of tumor suppressor in lung cancer 1 (TSLC1) binding to differentially expressed in adenocarcinoma of the lung (DAL-1/4.1B).,Busam RD, Thorsell AG, Flores A, Hammarstrom M, Persson C, Obrink B, Hallberg BM J Biol Chem. 2010 Dec 3. PMID:21131357 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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