3bin

<StructureSection load='3bin' size='340' side='right' caption='[[3bin]], [[Resolution|resolution]] 2.30&Aring;' scene=''>

<table><tr><td colspan='2'>[[3bin]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BIN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BIN FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2he7|2he7]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EPB41L3, DAL1, KIAA0987 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bin FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bin OCA], [http://pdbe.org/3bin PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bin RCSB], [http://www.ebi.ac.uk/pdbsum/3bin PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/E41L3_HUMAN E41L3_HUMAN]] Critical growth regulator in the pathogenesis of meningiomas. [[http://www.uniprot.org/uniprot/CADM1_HUMAN CADM1_HUMAN]] Mediates homophilic cell-cell adhesion in a Ca(2+)-independent manner. Also mediates heterophilic cell-cell adhesion with CADM3 and PVRL3 in a Ca(2+)-independent manner. Acts as a tumor suppressor in non-small-cell lung cancer (NSCLC) cells. Interaction with CRTAM promotes natural killer (NK) cell cytotoxicity and interferon-gamma (IFN-gamma) secretion by CD8+ cells in vitro as well as NK cell-mediated rejection of tumors expressing CADM3 in vivo. May contribute to the less invasive phenotypes of lepidic growth tumor cells. In mast cells, may mediate attachment to and promote communication with nerves. CADM1, together with MITF, is essential for development and survival of mast cells in vivo. May act as a synaptic cell adhesion molecule that drives synapse assembly. May be involved in neuronal migration, axon growth, pathfinding, and fasciculation on the axons of differentiating neurons. May play diverse roles in the spermatogenesis including in the adhesion of spermatocytes and spermatids to Sertoli cells and for their normal differentiation into mature spermatozoa.<ref>PMID:11279526</ref> <ref>PMID:12234973</ref> <ref>PMID:12050160</ref> <ref>PMID:12920246</ref> <ref>PMID:15811952</ref> <ref>PMID:15905536</ref> [UniProtKB:Q8R5M8]

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bi/3bin_consurf.spt"</scriptWhenChecked>

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== 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<ref>PMID:21131357</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 3bin" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Human]]

[[Category: Arrowsmith, C H]]

[[Category: Berg, S Van Den]]

[[Category: Berglund, H]]

[[Category: Busam, R D]]

[[Category: Collins, R]]

[[Category: Dahlgren, L G]]

[[Category: Edwards, A M]]

[[Category: Flodin, S]]

[[Category: Flores, A]]

[[Category: Graslund, S]]

[[Category: Hallberg, B M]]

[[Category: Hammarstrom, M]]

[[Category: Johansson, A]]

[[Category: Johansson, I]]

[[Category: Kallas, A]]

[[Category: Karlberg, T]]

[[Category: Kotenyova, T]]

[[Category: Lehtio, L]]

[[Category: Moche, M]]

[[Category: Nilsson, M E]]

[[Category: Nordlund, P]]

[[Category: Nyman, T]]

[[Category: Persson, C]]

[[Category: Sagemark, J]]

[[Category: Svensson, L]]

[[Category: Thorsell, A G]]

[[Category: Tresaugues, L]]

[[Category: Weigelt, J]]

[[Category: Welin, M]]

[[Category: Actin-binding]]

[[Category: Tslc1]]