1e0m

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[[Image:1e0m.gif|left|200px]]
 
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{{Structure
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==PROTOTYPE WW domain==
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|PDB= 1e0m |SIZE=350|CAPTION= <scene name='initialview01'>1e0m</scene>
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<StructureSection load='1e0m' size='340' side='right'caption='[[1e0m]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<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>
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|ACTIVITY=
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</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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|GENE=
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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>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Evolutionary Conservation ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e0m OCA], [http://www.ebi.ac.uk/pdbsum/1e0m PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e0m RCSB]</span>
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[[Image:Consurf_key_small.gif|200px|right]]
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}}
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Check<jmol>
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<jmolCheckbox>
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'''PROTOTYPE WW DOMAIN'''
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e0/1e0m_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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==Overview==
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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=1e0m 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 ==
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.
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==About this Structure==
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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>
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1E0M is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E0M OCA].
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==Reference==
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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]
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[[Category: ]]
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[[Category: Protein complex]]
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[[Category: Civera, C.]]
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[[Category: Gervais, V.]]
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[[Category: Macias, M J.]]
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[[Category: Oschkinat, H.]]
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[[Category: protein design]]
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[[Category: wwprototype]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:52:32 2008''
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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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<div class="pdbe-citations 1e0m" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Synthetic construct]]
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[[Category: Civera C]]
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[[Category: Gervais V]]
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[[Category: Macias MJ]]
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[[Category: Oschkinat H]]

Current revision

PROTOTYPE WW domain

PDB ID 1e0m

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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