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| | <StructureSection load='2wzo' size='340' side='right'caption='[[2wzo]], [[Resolution|resolution]] 1.60Å' scene=''> | | <StructureSection load='2wzo' size='340' side='right'caption='[[2wzo]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2wzo]] is a 1 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=2WZO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WZO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2wzo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WZO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WZO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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]] 1.6Å</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=2wzo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wzo OCA], [http://pdbe.org/2wzo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wzo RCSB], [http://www.ebi.ac.uk/pdbsum/2wzo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wzo ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=2wzo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wzo OCA], [https://pdbe.org/2wzo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wzo RCSB], [https://www.ebi.ac.uk/pdbsum/2wzo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wzo ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TBRG1_HUMAN TBRG1_HUMAN]] Acts as a growth inhibitor. Can activate p53/TP53, causes G1 arrest and collaborates with CDKN2A to restrict proliferation, but does not require either protein to inhibit DNA synthesis. Redistributes CDKN2A into the nucleoplasm. Involved in maintaining chromosomal stability.<ref>PMID:17110379</ref> | + | [https://www.uniprot.org/uniprot/TBRG1_HUMAN TBRG1_HUMAN] Acts as a growth inhibitor. Can activate p53/TP53, causes G1 arrest and collaborates with CDKN2A to restrict proliferation, but does not require either protein to inhibit DNA synthesis. Redistributes CDKN2A into the nucleoplasm. Involved in maintaining chromosomal stability.<ref>PMID:17110379</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Allen, M D]] | + | [[Category: Allen MD]] |
| - | [[Category: Bycroft, M]] | + | [[Category: Bycroft M]] |
| - | [[Category: Garcia-Alai, M M]] | + | [[Category: Garcia-Alai MM]] |
| - | [[Category: Joerger, A C]] | + | [[Category: Joerger AC]] |
| - | [[Category: Cell cycle]]
| + | |
| - | [[Category: Nucleus]]
| + | |
| - | [[Category: Tumor suppressor]]
| + | |
| Structural highlights
Function
TBRG1_HUMAN Acts as a growth inhibitor. Can activate p53/TP53, causes G1 arrest and collaborates with CDKN2A to restrict proliferation, but does not require either protein to inhibit DNA synthesis. Redistributes CDKN2A into the nucleoplasm. Involved in maintaining chromosomal stability.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Many chromatin-associated proteins contain two sequence motifs rich in phenylalanine/tyrosine residues of unknown function. These so called FYRN and FYRC motifs are also found in TBRG1 (transforming growth factor beta regulator 1)/ NIAM (Nuclear interactor of ARF and MDM2), a growth inhibitory protein that also plays a role in maintaining chromosomal stability. We have solved the structure of a fragment of TBRG1, which encompasses both of these motifs. The FYRN and FYRC regions each form part of a single folded module (the FYR domain), which adopts a novel alpha+beta fold. Proteins such as the histone H3K4 methyltransferases trithorax and mixed lineage leukemia (MLL), in which the FYRN and FYRC regions are separated by hundreds of amino acids, are expected to contain FYR domains with a large insertion between two of the strands of the beta-sheet.
The structure of the FYR domain of transforming growth factor beta regulator 1 (TBRG1).,Garcia-Alai MM, Allen MD, Joerger AC, Bycroft M Protein Sci. 2010 Apr 21. PMID:20506279[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tompkins VS, Hagen J, Frazier AA, Lushnikova T, Fitzgerald MP, di Tommaso A, Ladeveze V, Domann FE, Eischen CM, Quelle DE. A novel nuclear interactor of ARF and MDM2 (NIAM) that maintains chromosomal stability. J Biol Chem. 2007 Jan 12;282(2):1322-33. Epub 2006 Nov 16. PMID:17110379 doi:http://dx.doi.org/10.1074/jbc.M609612200
- ↑ Garcia-Alai MM, Allen MD, Joerger AC, Bycroft M. The structure of the FYR domain of transforming growth factor beta regulator 1 (TBRG1). Protein Sci. 2010 Apr 21. PMID:20506279 doi:10.1002/pro.404
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