1rut

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[[Image:1rut.png|left|200px]]
 
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==Complex of LMO4 LIM domains 1 and 2 with the ldb1 LID domain==
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The line below this paragraph, containing "STRUCTURE_1rut", creates the "Structure Box" on the page.
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<StructureSection load='1rut' size='340' side='right'caption='[[1rut]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1rut]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RUT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RUT FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_1rut| PDB=1rut | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rut OCA], [https://pdbe.org/1rut PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rut RCSB], [https://www.ebi.ac.uk/pdbsum/1rut PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rut ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LDB1_MOUSE LDB1_MOUSE] Binds to the LIM domain of a wide variety of LIM domain-containing transcription factors. May regulate the transcriptional activity of LIM-containing proteins by determining specific partner interactions. May play a role in the development of motor neurons. Acts synergistically with LHX1/LIM1 in axis formation and activation of gene expression. Acts with LMO2 in the regulation of red blood cell development, maintaining erythroid precursors in an immature state.<ref>PMID:8918878</ref> <ref>PMID:8876198</ref> <ref>PMID:9192866</ref> <ref>PMID:9391090</ref> <ref>PMID:16815859</ref> <ref>PMID:9315627</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ru/1rut_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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/main_output.php?pdb_ID=1rut ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Nuclear LIM-only (LMO) and LIM-homeodomain (LIM-HD) proteins have important roles in cell fate determination, organ development and oncogenesis. These proteins contain tandemly arrayed LIM domains that bind the LIM interaction domain (LID) of the nuclear adaptor protein LIM domain-binding protein-1 (Ldb1). We have determined a high-resolution X-ray crystal structure of LMO4, a putative breast oncoprotein, in complex with Ldb1-LID, providing the first example of a tandem LIM:Ldb1-LID complex and the first structure of a type-B LIM domain. The complex possesses a highly modular structure with Ldb1-LID binding in an extended manner across both LIM domains of LMO4. The interface contains extensive hydrophobic and electrostatic interactions and multiple backbone-backbone hydrogen bonds. A mutagenic screen of Ldb1-LID, assessed by yeast two-hybrid and competition ELISA analysis, identified key features at the interface and revealed that the interaction is tolerant to mutation. These combined properties provide a mechanism for the binding of Ldb1 to numerous LMO and LIM-HD proteins. Furthermore, the modular extended interface may form a general mode of binding to tandem LIM domains.
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===Complex of LMO4 LIM domains 1 and 2 with the ldb1 LID domain===
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Tandem LIM domains provide synergistic binding in the LMO4:Ldb1 complex.,Deane JE, Ryan DP, Sunde M, Maher MJ, Guss JM, Visvader JE, Matthews JM EMBO J. 2004 Sep 15;23(18):3589-98. Epub 2004 Sep 2. PMID:15343268<ref>PMID:15343268</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_15343268}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1rut" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 15343268 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15343268}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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[[1rut]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RUT OCA].
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==Reference==
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<ref group="xtra">PMID:15343268</ref><ref group="xtra">PMID:12876360</ref><references group="xtra"/>
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Bacca, M.]]
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[[Category: Bacca M]]
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[[Category: Deane, J E.]]
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[[Category: Deane JE]]
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[[Category: Guss, J M.]]
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[[Category: Guss JM]]
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[[Category: Kwan, A H.Y.]]
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[[Category: Kwan AHY]]
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[[Category: Mackay, J P.]]
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[[Category: Mackay JP]]
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[[Category: Maher, M J.]]
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[[Category: Maher MJ]]
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[[Category: Matthews, J M.]]
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[[Category: Matthews JM]]
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[[Category: Ryan, D P.]]
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[[Category: Ryan DP]]
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[[Category: Visvader, J E.]]
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[[Category: Visvader JE]]
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[[Category: B-tandem zipper]]
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[[Category: Fusion protein]]
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[[Category: Lim domain]]
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[[Category: Protein binding]]
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Current revision

Complex of LMO4 LIM domains 1 and 2 with the ldb1 LID domain

PDB ID 1rut

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OCA

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