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2lxd

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Revision as of 22:29, 9 August 2018

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

Structural highlights

2lxd is a 1 chain structure with sequence from Lk3 transgenic mice. 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.
Ligands:
Gene:	Lmo2, Ldb1 (LK3 transgenic mice)
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]

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^[2]

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
↑ 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:http://dx.doi.org/10.1002/pro.2153

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ 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=''>
@@ Line 5: / Line 6: @@
 </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>
 <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='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://pdbe.org/2lxd PDBe], [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'>[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://pdbe.org/2lxd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2lxd RCSB], [http://www.ebi.ac.uk/pdbsum/2lxd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2lxd ProSAT]</span></td></tr>
 </table>
 == Function ==

2lxd

From Proteopedia

Revision as of 22:29, 9 August 2018

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

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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