2lxd: Difference between revisions

Latest revision as of 05:54, 15 May 2024

Backbone 1H, 13C, and 15N Chemical Shift Assignments for LMO2(LIM2)-Ldb1(LID)

Structural highlights

2lxd is a 1 chain structure with sequence from Mus musculus. This structure supersedes the now removed PDB entry 2l3k. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Ligands:	ZN
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RBTN2_MOUSE Acts with TAL1/SCL to regulate red blood cell development. Also acts with LDB1 to maintain erythroid precursors in an immature state.^[1] 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.^[2] ^[3] ^[4] ^[5] ^[6] ^[7]

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^[8]

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

References

↑ Visvader JE, Mao X, Fujiwara Y, Hahm K, Orkin SH. The LIM-domain binding protein Ldb1 and its partner LMO2 act as negative regulators of erythroid differentiation. Proc Natl Acad Sci U S A. 1997 Dec 9;94(25):13707-12. PMID:9391090
↑ Agulnick AD, Taira M, Breen JJ, Tanaka T, Dawid IB, Westphal H. Interactions of the LIM-domain-binding factor Ldb1 with LIM homeodomain proteins. Nature. 1996 Nov 21;384(6606):270-2. PMID:8918878 doi:https://dx.doi.org/10.1038/384270a0
↑ Jurata LW, Kenny DA, Gill GN. Nuclear LIM interactor, a rhombotin and LIM homeodomain interacting protein, is expressed early in neuronal development. Proc Natl Acad Sci U S A. 1996 Oct 15;93(21):11693-8. PMID:8876198
↑ Bach I, Carriere C, Ostendorff HP, Andersen B, Rosenfeld MG. A family of LIM domain-associated cofactors confer transcriptional synergism between LIM and Otx homeodomain proteins. Genes Dev. 1997 Jun 1;11(11):1370-80. PMID:9192866
↑ Visvader JE, Mao X, Fujiwara Y, Hahm K, Orkin SH. The LIM-domain binding protein Ldb1 and its partner LMO2 act as negative regulators of erythroid differentiation. Proc Natl Acad Sci U S A. 1997 Dec 9;94(25):13707-12. PMID:9391090
↑ Tran YH, Xu Z, Kato A, Mistry AC, Goya Y, Taira M, Brandt SJ, Hirose S. Spliced isoforms of LIM-domain-binding protein (CLIM/NLI/Ldb) lacking the LIM-interaction domain. J Biochem. 2006 Jul;140(1):105-19. Epub 2006 Jun 30. PMID:16815859 doi:https://dx.doi.org/10.1093/jb/mvj134
↑ Jurata LW, Gill GN. Functional analysis of the nuclear LIM domain interactor NLI. Mol Cell Biol. 1997 Oct;17(10):5688-98. PMID:9315627
↑ Dastmalchi S, Wilkinson-White L, Kwan AH, Gamsjaeger R, Mackay JP, Matthews JM. Solution structure of a tethered Lmo2(LIM2) /Ldb1(LID) complex. Protein Sci. 2012 Aug 30. doi: 10.1002/pro.2153. PMID:22936624 doi:https://dx.doi.org/10.1002/pro.2153

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Visvader JE, Mao X, Fujiwara Y, Hahm K, Orkin SH. The LIM-domain binding protein Ldb1 and its partner LMO2 act as negative regulators of erythroid differentiation. Proc Natl Acad Sci U S A. 1997 Dec 9;94(25):13707-12. PMID:9391090

[2] Agulnick AD, Taira M, Breen JJ, Tanaka T, Dawid IB, Westphal H. Interactions of the LIM-domain-binding factor Ldb1 with LIM homeodomain proteins. Nature. 1996 Nov 21;384(6606):270-2. PMID:8918878 doi:https://dx.doi.org/10.1038/384270a0

[3] Jurata LW, Kenny DA, Gill GN. Nuclear LIM interactor, a rhombotin and LIM homeodomain interacting protein, is expressed early in neuronal development. Proc Natl Acad Sci U S A. 1996 Oct 15;93(21):11693-8. PMID:8876198

[4] Bach I, Carriere C, Ostendorff HP, Andersen B, Rosenfeld MG. A family of LIM domain-associated cofactors confer transcriptional synergism between LIM and Otx homeodomain proteins. Genes Dev. 1997 Jun 1;11(11):1370-80. PMID:9192866

[5] Visvader JE, Mao X, Fujiwara Y, Hahm K, Orkin SH. The LIM-domain binding protein Ldb1 and its partner LMO2 act as negative regulators of erythroid differentiation. Proc Natl Acad Sci U S A. 1997 Dec 9;94(25):13707-12. PMID:9391090

[6] Tran YH, Xu Z, Kato A, Mistry AC, Goya Y, Taira M, Brandt SJ, Hirose S. Spliced isoforms of LIM-domain-binding protein (CLIM/NLI/Ldb) lacking the LIM-interaction domain. J Biochem. 2006 Jul;140(1):105-19. Epub 2006 Jun 30. PMID:16815859 doi:https://dx.doi.org/10.1093/jb/mvj134

[7] Jurata LW, Gill GN. Functional analysis of the nuclear LIM domain interactor NLI. Mol Cell Biol. 1997 Oct;17(10):5688-98. PMID:9315627

[8] Dastmalchi S, Wilkinson-White L, Kwan AH, Gamsjaeger R, Mackay JP, Matthews JM. Solution structure of a tethered Lmo2(LIM2) /Ldb1(LID) complex. Protein Sci. 2012 Aug 30. doi: 10.1002/pro.2153. PMID:22936624 doi:https://dx.doi.org/10.1002/pro.2153

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[5]

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[8]

@@ Line 1: / Line 1: @@
 ==Backbone 1H, 13C, and 15N Chemical Shift Assignments for LMO2(LIM2)-Ldb1(LID)==
-<StructureSection load='2lxd' size='340' side='right' caption='[[2lxd]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2lxd' size='340' side='right'caption='[[2lxd]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2lxd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LXD FirstGlance]. <br>
+<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Lmo2, Ldb1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2lxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lxd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lxd RCSB], [http://www.ebi.ac.uk/pdbsum/2lxd PDBsum]</span></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>
+== 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 ==
@@ Line 15: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, 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__
 </StructureSection>
-[[Category: Lk3 transgenic mice]]
+[[Category: Large Structures]]
-[[Category: Dastmalchi, S]]
+[[Category: Mus musculus]]
-[[Category: Gamsjaeger, R]]
+[[Category: Dastmalchi S]]
-[[Category: Kwan, A H]]
+[[Category: Gamsjaeger R]]
-[[Category: Mackay, J P]]
+[[Category: Kwan AH]]
-[[Category: Matthews, J M]]
+[[Category: Mackay JP]]
-[[Category: Wilkinson-White, L]]
+[[Category: Matthews JM]]
-[[Category: Ldb1]]
+[[Category: Wilkinson-White L]]
-[[Category: Lim]]
-[[Category: Transcription]]

2lxd: Difference between revisions

Latest revision as of 05:54, 15 May 2024

Backbone 1H, 13C, and 15N Chemical Shift Assignments for LMO2(LIM2)-Ldb1(LID)

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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