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| | ==FBP28WW domain from Mus musculus== | | ==FBP28WW domain from Mus musculus== |
| - | <StructureSection load='1e0l' size='340' side='right' caption='[[1e0l]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='1e0l' size='340' side='right'caption='[[1e0l]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1e0l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E0L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E0L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1e0l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E0L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E0L FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e0m|1e0m]], [[1e0n|1e0n]]</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='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=1e0l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e0l OCA], [http://pdbe.org/1e0l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e0l RCSB], [http://www.ebi.ac.uk/pdbsum/1e0l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1e0l 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=1e0l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e0l OCA], [https://pdbe.org/1e0l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e0l RCSB], [https://www.ebi.ac.uk/pdbsum/1e0l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e0l ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TCRG1_MOUSE TCRG1_MOUSE]] Transcription factor that binds RNA polymerase II and inhibits the elongation of transcripts from target promoters. Regulates transcription elongation in a TATA box-dependent manner (By similarity). | + | [https://www.uniprot.org/uniprot/TCRG1_MOUSE TCRG1_MOUSE] Transcription factor that binds RNA polymerase II and inhibits the elongation of transcripts from target promoters. Regulates transcription elongation in a TATA box-dependent manner (By similarity). |
| | == 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: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
| - | [[Category: Civera, C]] | + | [[Category: Mus musculus]] |
| - | [[Category: Gervais, V]] | + | [[Category: Civera C]] |
| - | [[Category: Macias, M J]] | + | [[Category: Gervais V]] |
| - | [[Category: Oschkinat, H]] | + | [[Category: Macias MJ]] |
| - | [[Category: Fbp28]]
| + | [[Category: Oschkinat H]] |
| - | [[Category: Sh3 domain]]
| + | |
| - | [[Category: Signal transduction]]
| + | |
| - | [[Category: Ww domain]]
| + | |
| Structural highlights
Function
TCRG1_MOUSE Transcription factor that binds RNA polymerase II and inhibits the elongation of transcripts from target promoters. Regulates transcription elongation in a TATA box-dependent manner (By similarity).
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
Two new NMR structures of WW domains, the mouse formin binding protein and a putative 84.5 kDa protein from Saccharomyces cerevisiae, show that this domain, only 35 amino acids in length, defines the smallest monomeric triple-stranded antiparallel beta-sheet protein domain that is stable in the absence of disulfide bonds, tightly bound ions or ligands. The structural roles of conserved residues have been studied using site-directed mutagenesis of both wild type domains. Crucial interactions responsible for the stability of the WW structure have been identified. Based on a network of highly conserved long range interactions across the beta-sheet structure that supports the WW fold and on a systematic analysis of conserved residues in the WW family, we have designed a folded prototype WW sequence.
Structural analysis of WW domains and design of a WW prototype.,Macias MJ, Gervais V, Civera C, Oschkinat H Nat Struct Biol. 2000 May;7(5):375-9. PMID:10802733[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Macias MJ, Gervais V, Civera C, Oschkinat H. Structural analysis of WW domains and design of a WW prototype. Nat Struct Biol. 2000 May;7(5):375-9. PMID:10802733 doi:10.1038/75144
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