2lxd
From Proteopedia
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<StructureSection load='2lxd' size='340' side='right'caption='[[2lxd]]' scene=''> | <StructureSection load='2lxd' size='340' side='right'caption='[[2lxd]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2l3k 2l3k]. Full | + | <table><tr><td colspan='2'>[[2lxd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2l3k 2l3k]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LXD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LXD FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2lxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lxd OCA], [https://pdbe.org/2lxd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lxd RCSB], [https://www.ebi.ac.uk/pdbsum/2lxd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lxd ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| + | <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> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2lxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lxd OCA], [https://pdbe.org/2lxd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lxd RCSB], [https://www.ebi.ac.uk/pdbsum/2lxd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lxd ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/RBTN2_MOUSE RBTN2_MOUSE] Acts with TAL1/SCL to regulate red blood cell development. Also acts with LDB1 to maintain erythroid precursors in an immature state.<ref>PMID:9391090</ref> [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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | LIM-only protein 2, Lmo2, is a regulatory protein that is essential for hematopoietic development and inappropriate overexpression of Lmo2 in T cells contributes to T cell leukaemia. It exerts its functions by mediating protein-protein interactions and nucleating multicomponent transcriptional complexes. Lmo2 interacts with LIM domain binding protein 1 (Ldb1) through the tandem LIM domains of Lmo2 and the LIM interaction domain (LID) of Ldb1. Here we present the solution structure of the LIM2 domain of Lmo2 bound to Ldb1(LID) . The ordered regions of Ldb1 in this complex correspond well with binding hotspots previously defined by mutagenic studies. Comparisons of this Lmo2(LIM2) -Ldb1(LID) structure with previously determined structures of the Lmo2/Ldb1(LID) complexes lead to the conclusion that modular binding of tandem LIM domains in Lmo2 to tandem linear motifs in Ldb1 is accompanied by several disorder-to-order transitions and/or conformational changes in both proteins. Proteins 2012. (c) 2012 The Protein Society. | ||
| + | |||
| + | Solution structure of a tethered Lmo2(LIM2) /Ldb1(LID) complex.,Dastmalchi S, Wilkinson-White L, Kwan AH, Gamsjaeger R, Mackay JP, Matthews JM Protein Sci. 2012 Aug 30. doi: 10.1002/pro.2153. PMID:22936624<ref>PMID:22936624</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2lxd" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Mus musculus]] | ||
[[Category: Dastmalchi S]] | [[Category: Dastmalchi S]] | ||
[[Category: Gamsjaeger R]] | [[Category: Gamsjaeger R]] | ||
Current revision
Backbone 1H, 13C, and 15N Chemical Shift Assignments for LMO2(LIM2)-Ldb1(LID)
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