3bin: Difference between revisions
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[[Image: | ==Structure of the DAL-1 and TSLC1 (372-383) complex== | ||
<StructureSection load='3bin' size='340' side='right' caption='[[3bin]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3bin]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2he7|2he7]]</td></tr> | |||
<tr><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 Homo sapiens])</td></tr> | |||
<tr><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://www.rcsb.org/pdb/explore.do?structureId=3bin RCSB], [http://www.ebi.ac.uk/pdbsum/3bin PDBsum]</span></td></tr> | |||
<table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bi/3bin_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Arrowsmith, C H.]] | [[Category: Arrowsmith, C H.]] |
Revision as of 00:08, 3 October 2014
Structure of the DAL-1 and TSLC1 (372-383) complexStructure of the DAL-1 and TSLC1 (372-383) complex
Structural highlights
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 PubMedPerturbed 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Homo sapiens
- Arrowsmith, C H.
- Berg, S Van Den.
- Berglund, H.
- Busam, R D.
- Collins, R.
- Dahlgren, L G.
- Edwards, A M.
- Flodin, S.
- Flores, A.
- Graslund, S.
- Hallberg, B M.
- Hammarstrom, M.
- Johansson, A.
- Johansson, I.
- Kallas, A.
- Karlberg, T.
- Kotenyova, T.
- Lehtio, L.
- Moche, M.
- Nilsson, M E.
- Nordlund, P.
- Nyman, T.
- Persson, C.
- Sagemark, J.
- Svensson, L.
- Thorsell, A G.
- Tresaugues, L.
- Weigelt, J.
- Welin, M.
- Actin-binding
- Anti-oncogene
- Apoptosis
- Cell adhesion
- Cell cycle
- Cytoskeleton
- Dal-1
- Developmental protein
- Differentiation
- Ferm domain
- Glycoprotein
- Immune response
- Immunoglobulin domain
- Membrane
- Phosphoprotein
- Spermatogenesis
- Structural protein
- Transmembrane
- Tslc1