This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2he7

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 06:43, 27 June 2018

FERM domain of EPB41L3 (DAL-1)

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Busam RD, Thorsell AG, Flores A, Hammarstrom M, Persson C, Obrink B, Hallberg BM. 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. 2010 Dec 3. PMID:21131357 doi:10.1074/jbc.M110.174011

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2he7"

@@ Line 1: / Line 1: @@
 ==FERM domain of EPB41L3 (DAL-1)==
 <StructureSection load='2he7' size='340' side='right' caption='[[2he7]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[2he7]] is a 1 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=2HE7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HE7 FirstGlance]. <br>
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EPB41L3 ([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=2he7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2he7 OCA], [http://pdbe.org/2he7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2he7 RCSB], [http://www.ebi.ac.uk/pdbsum/2he7 PDBsum]</span></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=2he7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2he7 OCA], [http://pdbe.org/2he7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2he7 RCSB], [http://www.ebi.ac.uk/pdbsum/2he7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2he7 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 12: / Line 13: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/he/2he7_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/he/2he7_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2he7

From Proteopedia

Revision as of 06:43, 27 June 2018

FERM domain of EPB41L3 (DAL-1)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox