View source for 1ywi


==Structure of the FBP11WW1 domain complexed to the peptide APPTPPPLPP==
<StructureSection load='1ywi' size='340' side='right'caption='[[1ywi]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ywi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YWI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YWI FirstGlance]. <br>
</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=1ywi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ywi OCA], [https://pdbe.org/1ywi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ywi RCSB], [https://www.ebi.ac.uk/pdbsum/1ywi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ywi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PR40A_HUMAN PR40A_HUMAN] Binds to WASL/N-WASP and suppresses its translocation from the nucleus to the cytoplasm, thereby inhibiting its cytoplasmic function (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. May play a role in cytokinesis. May be involved in pre-mRNA splicing.<ref>PMID:21834987</ref> 
== 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/yw/1ywi_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=1ywi ConSurf].
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== Publication Abstract from PubMed ==
WW domains are small protein-protein interaction modules that recognize proline-rich stretches in proteins. The class II tandem WW domains of the formin binding protein 11 (FBP11) recognize specifically proteins containing PPLPp motifs as present in the formins that are involved in limb and kidney development, and in the methyl-CpG-binding protein 2 (MeCP2), associated with the Rett syndrome. The interaction involves the specific recognition of a leucine side-chain. Here, we report on the novel structure of the complex formed by the FPB11WW1 domain and the formin fragment APPTPPPLPP revealing the specificity determinants of class II WW domains.

Structural basis for APPTPPPLPP peptide recognition by the FBP11WW1 domain.,Pires JR, Parthier C, Aido-Machado R, Wiedemann U, Otte L, Bohm G, Rudolph R, Oschkinat H J Mol Biol. 2005 Apr 29;348(2):399-408. PMID:15811376<ref>PMID:15811376</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1ywi" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Aido-Machado R]]
[[Category: Boehm G]]
[[Category: Oschkinat H]]
[[Category: Otte L]]
[[Category: Parthier C]]
[[Category: Pires JR]]
[[Category: Rudolph R]]
[[Category: Wiedemann U]]