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| | ==FBP28WW2 domain in complex with PTPPPLPP peptide== | | ==FBP28WW2 domain in complex with PTPPPLPP peptide== |
| - | <StructureSection load='2rly' size='340' side='right'caption='[[2rly]], [[NMR_Ensembles_of_Models | 8 NMR models]]' scene=''> | + | <StructureSection load='2rly' size='340' side='right'caption='[[2rly]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2rly]] is a 2 chain structure with sequence from [https://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=2RLY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RLY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2rly]] is a 2 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=2RLY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RLY FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2jup|2jup]], [[2rm0|2rm0]]</div></td></tr> | + | </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=2rly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rly OCA], [https://pdbe.org/2rly PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rly RCSB], [https://www.ebi.ac.uk/pdbsum/2rly PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rly ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tcerg1, Taf2s ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2rly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rly OCA], [https://pdbe.org/2rly PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rly RCSB], [https://www.ebi.ac.uk/pdbsum/2rly PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rly ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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). [[https://www.uniprot.org/uniprot/FMN1_MOUSE FMN1_MOUSE]] Plays a role in the formation of adherens junction and the polymerization of linear actin cables.<ref>PMID:15198975</ref> <ref>PMID:14647292</ref>
| + | [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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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Macias, M J]] | + | [[Category: Macias MJ]] |
| - | [[Category: Martin-Malpartida, P]] | + | [[Category: Martin-Malpartida P]] |
| - | [[Category: Oschkinat, H]] | + | [[Category: Oschkinat H]] |
| - | [[Category: Ramirez-Espain, X]] | + | [[Category: Ramirez-Espain X]] |
| - | [[Category: Ruiz, L]] | + | [[Category: Ruiz L]] |
| - | [[Category: Actin-binding]]
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| - | [[Category: Alternative splicing]]
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| - | [[Category: Cell junction]]
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| - | [[Category: Coiled coil]]
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| - | [[Category: Cytoplasm]]
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| - | [[Category: Fbp28ww domain]]
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| - | [[Category: Membrane]]
| + | |
| - | [[Category: Nucleus]]
| + | |
| - | [[Category: Phosphorylation]]
| + | |
| - | [[Category: Polymorphism]]
| + | |
| - | [[Category: Ptppplpp peptide]]
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| - | [[Category: Repressor]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Transcription regulation]]
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| 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
Formin homology 1 (FH1), is a long proline-rich region of formins, shown to bind to five WW containing proteins named formin binding proteins (FBPs). FH1 has several potential binding regions but only the PPLPx motif and its interaction with FBP11WW1 has been characterized structurally. To detect whether additional motifs exist in FH1, we synthesized five peptides and investigated their interaction with FBP28WW2, FBP11WW1 and FBP11WW2 domains. Peptides of sequence PTPPPLPP (positive control), PPPLIPPPP and PPLIPPPP (new motifs) interact with the domains with micromolar affinity. We observed that FBP28WW2 and FBP11WW2 behave differently from FBP11WW1 in terms of motif selection and affinity, since they prefer a doubly interrupted proline stretch of sequence PPLIPP. We determined the NMR structure of three complexes involving the FBP28WW2 domain and the three ligands. Depending on the peptide under study, the domain interacts with two proline residues accommodated in either the XP or the XP2 groove. This difference represents a one-turn displacement of the domain along the ligand sequence. To understand what drives this behavior, we performed further structural studies with the FBP11WW1 and a mutant of FBP28WW2 mimicking the XP2 groove of FBP11WW1. Our observations suggest that the nature of the XP2 groove and the balance of flexibility/rigidity around loop 1 of the domain contribute to the selection of the final ligand positioning in fully independent domains. Additionally, we analyzed the binding of a double WW domain region, FBP11WW1-2, to a long stretch of FH1 using fluorescence spectroscopy and NMR titrations. With this we show that the presence of two consecutive WW domains may also influence the selection of the binding mode, particularly if both domains can interact with consecutive motifs in the ligand. Our results represent the first observation of protein-ligand recognition where a pair of WW and two consecutive motifs in a ligand participate simultaneously.
Structural characterization of a new binding motif and a novel binding mode in group 2 WW domains.,Ramirez-Espain X, Ruiz L, Martin-Malpartida P, Oschkinat H, Macias MJ J Mol Biol. 2007 Nov 9;373(5):1255-68. Epub 2007 Aug 29. PMID:17915251[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ramirez-Espain X, Ruiz L, Martin-Malpartida P, Oschkinat H, Macias MJ. Structural characterization of a new binding motif and a novel binding mode in group 2 WW domains. J Mol Biol. 2007 Nov 9;373(5):1255-68. Epub 2007 Aug 29. PMID:17915251 doi:10.1016/j.jmb.2007.08.052
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