2rm0

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{{Seed}}
 
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[[Image:2rm0.png|left|200px]]
 
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==FBP28WW2 domain in complex with a PPPLIPPPP peptide==
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The line below this paragraph, containing "STRUCTURE_2rm0", creates the "Structure Box" on the page.
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<StructureSection load='2rm0' size='340' side='right'caption='[[2rm0]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2rm0]] 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=2RM0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RM0 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</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=2rm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rm0 OCA], [https://pdbe.org/2rm0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rm0 RCSB], [https://www.ebi.ac.uk/pdbsum/2rm0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rm0 ProSAT]</span></td></tr>
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</table>
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{{STRUCTURE_2rm0| PDB=2rm0 | SCENE= }}
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== Function ==
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[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).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rm/2rm0_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2rm0 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===FBP28WW2 domain in complex with a PPPLIPPPP peptide===
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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<ref>PMID:17915251</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_17915251}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2rm0" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 17915251 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17915251}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2RM0 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RM0 OCA].
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==Reference==
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<ref group="xtra">PMID:17915251</ref><references group="xtra"/>
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Macias, M J.]]
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[[Category: Macias MJ]]
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[[Category: Martin-Malpartida, P.]]
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[[Category: Martin-Malpartida P]]
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[[Category: Oschkinat, H.]]
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[[Category: Oschkinat H]]
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[[Category: Ramirez-Espain, X.]]
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[[Category: Ramirez-Espain X]]
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[[Category: Ruiz, L.]]
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[[Category: Ruiz L]]
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[[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: Fbp28ww2]]
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[[Category: Membrane]]
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[[Category: Nmr]]
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[[Category: Nucleus]]
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[[Category: Phosphorylation]]
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[[Category: Polymorphism]]
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[[Category: Ppplipppp ligand]]
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[[Category: Repressor]]
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[[Category: Transcription]]
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[[Category: Transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 06:54:15 2009''
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Current revision

FBP28WW2 domain in complex with a PPPLIPPPP peptide

PDB ID 2rm0

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