1e0m: Difference between revisions
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==PROTOTYPE WW domain== | ==PROTOTYPE WW domain== | ||
<StructureSection load='1e0m' size='340' side='right' caption='[[1e0m]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | <StructureSection load='1e0m' size='340' side='right' caption='[[1e0m]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | ||
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<table><tr><td colspan='2'>[[1e0m]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E0M FirstGlance]. <br> | <table><tr><td colspan='2'>[[1e0m]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E0M FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e0l|1e0l]], [[1e0n|1e0n]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e0l|1e0l]], [[1e0n|1e0n]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1e0m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e0m RCSB], [http://www.ebi.ac.uk/pdbsum/1e0m PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1e0m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e0m RCSB], [http://www.ebi.ac.uk/pdbsum/1e0m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1e0m ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | </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="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Revision as of 06:54, 6 September 2017
PROTOTYPE WW domainPROTOTYPE WW domain
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedTwo 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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