|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5eg0' size='340' side='right'caption='[[5eg0]], [[Resolution|resolution]] 3.10Å' scene=''> | | <StructureSection load='5eg0' size='340' side='right'caption='[[5eg0]], [[Resolution|resolution]] 3.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5eg0]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EG0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5EG0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5eg0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EG0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EG0 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MEIS2, MRG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), HOXB13 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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]] 3.101Å</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=5eg0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5eg0 OCA], [http://pdbe.org/5eg0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5eg0 RCSB], [http://www.ebi.ac.uk/pdbsum/5eg0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5eg0 ProSAT]</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=5eg0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5eg0 OCA], [https://pdbe.org/5eg0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5eg0 RCSB], [https://www.ebi.ac.uk/pdbsum/5eg0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5eg0 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HXB13_HUMAN HXB13_HUMAN]] Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. [[http://www.uniprot.org/uniprot/MEIS2_HUMAN MEIS2_HUMAN]] Involved in transcriptional regulation. Binds to HOX or PBX proteins to form dimers, or to a DNA-bound dimer of PBX and HOX proteins and thought to have a role in stabilization of the homeoprotein-DNA complex. Isoform 3/Meis2B is required for the activity of a PDX1:PBX1b:MEIS2b complex in pancreatic acinar cells involved in the transcriptional activation of the ELA1 enhancer; the complex binds to the enhancer B element and cooperates with the transcription factor 1 complex (PTF1) bound to the enhancer A element; MEIS2 is not involved in complex DNA-binding. Probably in complex with PBX1, is involved in transcriptional regulation by KLF4. Isoform 3/Meis2B and isoform 4/Meis2D can bind to a EPHA8 promoter sequence containing the DNA motif 5'-CGGTCA-3'; in cooperation with a PBX protein (such as PBX2) is proposed to be involved in the transcriptional activation of EPHA8 in the developing midbrain. May be involved in regulation of myeloid differentiation. Can bind to the DNA sequence 5'-TGACAG-3'in the activator ACT sequence of the D(1A) dopamine receptor (DRD1) promoter and activate DRD1 transcription; isoform 5/Meis2E cannot activate DRD1 transcription.<ref>PMID:10764806</ref> <ref>PMID:11279116</ref> <ref>PMID:21746878</ref> | + | [https://www.uniprot.org/uniprot/MEIS2_HUMAN MEIS2_HUMAN] Involved in transcriptional regulation. Binds to HOX or PBX proteins to form dimers, or to a DNA-bound dimer of PBX and HOX proteins and thought to have a role in stabilization of the homeoprotein-DNA complex. Isoform 3/Meis2B is required for the activity of a PDX1:PBX1b:MEIS2b complex in pancreatic acinar cells involved in the transcriptional activation of the ELA1 enhancer; the complex binds to the enhancer B element and cooperates with the transcription factor 1 complex (PTF1) bound to the enhancer A element; MEIS2 is not involved in complex DNA-binding. Probably in complex with PBX1, is involved in transcriptional regulation by KLF4. Isoform 3/Meis2B and isoform 4/Meis2D can bind to a EPHA8 promoter sequence containing the DNA motif 5'-CGGTCA-3'; in cooperation with a PBX protein (such as PBX2) is proposed to be involved in the transcriptional activation of EPHA8 in the developing midbrain. May be involved in regulation of myeloid differentiation. Can bind to the DNA sequence 5'-TGACAG-3'in the activator ACT sequence of the D(1A) dopamine receptor (DRD1) promoter and activate DRD1 transcription; isoform 5/Meis2E cannot activate DRD1 transcription.<ref>PMID:10764806</ref> <ref>PMID:11279116</ref> <ref>PMID:21746878</ref> |
| | | | |
| | ==See Also== | | ==See Also== |
| Line 16: |
Line 16: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Jolma, A]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Morgunova, E]] | + | [[Category: Jolma A]] |
| - | [[Category: Popov, A]] | + | [[Category: Morgunova E]] |
| - | [[Category: Taipale, J]] | + | [[Category: Popov A]] |
| - | [[Category: Yin, Y]] | + | [[Category: Taipale J]] |
| - | [[Category: Bound to dna]]
| + | [[Category: Yin Y]] |
| - | [[Category: Complex]]
| + | |
| - | [[Category: Heterodimer]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Transcription factor]]
| + | |
| Structural highlights
Function
MEIS2_HUMAN Involved in transcriptional regulation. Binds to HOX or PBX proteins to form dimers, or to a DNA-bound dimer of PBX and HOX proteins and thought to have a role in stabilization of the homeoprotein-DNA complex. Isoform 3/Meis2B is required for the activity of a PDX1:PBX1b:MEIS2b complex in pancreatic acinar cells involved in the transcriptional activation of the ELA1 enhancer; the complex binds to the enhancer B element and cooperates with the transcription factor 1 complex (PTF1) bound to the enhancer A element; MEIS2 is not involved in complex DNA-binding. Probably in complex with PBX1, is involved in transcriptional regulation by KLF4. Isoform 3/Meis2B and isoform 4/Meis2D can bind to a EPHA8 promoter sequence containing the DNA motif 5'-CGGTCA-3'; in cooperation with a PBX protein (such as PBX2) is proposed to be involved in the transcriptional activation of EPHA8 in the developing midbrain. May be involved in regulation of myeloid differentiation. Can bind to the DNA sequence 5'-TGACAG-3'in the activator ACT sequence of the D(1A) dopamine receptor (DRD1) promoter and activate DRD1 transcription; isoform 5/Meis2E cannot activate DRD1 transcription.[1] [2] [3]
See Also
References
- ↑ Yang Y, Hwang CK, D'Souza UM, Lee SH, Junn E, Mouradian MM. Three-amino acid extension loop homeodomain proteins Meis2 and TGIF differentially regulate transcription. J Biol Chem. 2000 Jul 7;275(27):20734-41. PMID:10764806 doi:10.1074/jbc.M908382199
- ↑ Liu Y, MacDonald RJ, Swift GH. DNA binding and transcriptional activation by a PDX1.PBX1b.MEIS2b trimer and cooperation with a pancreas-specific basic helix-loop-helix complex. J Biol Chem. 2001 May 25;276(21):17985-93. Epub 2001 Mar 13. PMID:11279116 doi:10.1074/jbc.M100678200
- ↑ Bjerke GA, Hyman-Walsh C, Wotton D. Cooperative transcriptional activation by Klf4, Meis2, and Pbx1. Mol Cell Biol. 2011 Sep;31(18):3723-33. doi: 10.1128/MCB.01456-10. Epub 2011 Jul , 11. PMID:21746878 doi:10.1128/MCB.01456-10
|
