6ptl: Difference between revisions

Latest revision as of 14:55, 13 March 2024

Structure of the self-association domain of the chromatin looping factor LDB1

Structural highlights

6ptl is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.5Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

References

↑ 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

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OCA

[1] 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

[2] 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

[3] 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

[4] 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

[5] 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

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

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@@ Line 1: / Line 1: @@
 ==Structure of the self-association domain of the chromatin looping factor LDB1==
-<StructureSection load='6ptl' size='340' side='right'caption='[[6ptl]]' scene=''>
+<StructureSection load='6ptl' size='340' side='right'caption='[[6ptl]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PTL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6PTL FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6ptl]] 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=6PTL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PTL FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6ptl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ptl OCA], [http://pdbe.org/6ptl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ptl RCSB], [http://www.ebi.ac.uk/pdbsum/6ptl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ptl ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</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=6ptl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ptl OCA], [https://pdbe.org/6ptl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ptl RCSB], [https://www.ebi.ac.uk/pdbsum/6ptl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ptl ProSAT]</span></td></tr>
 </table>
+== Function ==
+[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>
+== References ==
+<references/>
 __TOC__
 </StructureSection>
 [[Category: Large Structures]]
+[[Category: Mus musculus]]
 [[Category: Guss JM]]
 [[Category: Macindoe I]]

6ptl: Difference between revisions

Latest revision as of 14:55, 13 March 2024

Structure of the self-association domain of the chromatin looping factor LDB1

Structural highlights

Function

References

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