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[[Image:1e0m.gif|left|200px]]


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==PROTOTYPE WW domain==
The line below this paragraph, containing "STRUCTURE_1e0m", creates the "Structure Box" on the page.
<StructureSection load='1e0m' size='340' side='right'caption='[[1e0m]]' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1e0m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E0M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E0M FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1e0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e0m OCA], [https://pdbe.org/1e0m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e0m RCSB], [https://www.ebi.ac.uk/pdbsum/1e0m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e0m ProSAT]</span></td></tr>
{{STRUCTURE_1e0m| PDB=1e0m  | SCENE= }}
</table>
 
== Evolutionary Conservation ==
'''PROTOTYPE WW DOMAIN'''
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
 
  <jmolCheckbox>
==Overview==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e0/1e0m_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=1e0m ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.
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.


==About this Structure==
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<ref>PMID:10802733</ref>
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E0M OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://www.ncbi.nlm.nih.gov/pubmed/10802733 10802733]
</div>
[[Category: Civera, C.]]
<div class="pdbe-citations 1e0m" style="background-color:#fffaf0;"></div>
[[Category: Gervais, V.]]
== References ==
[[Category: Macias, M J.]]
<references/>
[[Category: Oschkinat, H.]]
__TOC__
[[Category: Protein design]]
</StructureSection>
[[Category: Wwprototype]]
[[Category: Large Structures]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:30:45 2008''
[[Category: Synthetic construct]]
[[Category: Civera C]]
[[Category: Gervais V]]
[[Category: Macias MJ]]
[[Category: Oschkinat H]]

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