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New page: left|200px<br /><applet load="2jup" size="350" color="white" frame="true" align="right" spinBox="true" caption="2jup" /> '''FBP28WW2 domain in complex with the PPLIPPPP...
 
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[[Image:2jup.jpg|left|200px]]<br /><applet load="2jup" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2jup" />
'''FBP28WW2 domain in complex with the PPLIPPPP peptide'''<br />


==Overview==
==FBP28WW2 domain in complex with the PPLIPPPP peptide==
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.
<StructureSection load='2jup' size='340' side='right'caption='[[2jup]]' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[2jup]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JUP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JUP FirstGlance]. <br>
2JUP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JUP OCA].  
</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'>[https://proteopedia.org/fgij/fg.htm?mol=2jup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jup OCA], [https://pdbe.org/2jup PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jup RCSB], [https://www.ebi.ac.uk/pdbsum/2jup PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jup ProSAT]</span></td></tr>
==Reference==
</table>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17915251 17915251]
== 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).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ju/2jup_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2jup ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Synthetic construct]]
[[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]]
[[Category: alternative splicing]]
[[Category: cell junction]]
[[Category: coiled coil]]
[[Category: cytoplasm]]
[[Category: fbp28ww domain]]
[[Category: membrane]]
[[Category: nmr]]
[[Category: nucleus]]
[[Category: phosphorylation]]
[[Category: polymorphism]]
[[Category: pplipppp peptide]]
[[Category: repressor]]
[[Category: transcription]]
[[Category: transcription regulation]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:21:17 2008''

Latest revision as of 06:42, 1 May 2024

FBP28WW2 domain in complex with the PPLIPPPP peptide

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