1e0m: Difference between revisions
New page: left|200px<br /><applet load="1e0m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e0m" /> '''PROTOTYPE WW DOMAIN'''<br /> ==Overview== T... |
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[[Image:1e0m.gif|left|200px]]<br /><applet load="1e0m" size=" | [[Image:1e0m.gif|left|200px]]<br /><applet load="1e0m" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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'''PROTOTYPE WW DOMAIN'''<br /> | '''PROTOTYPE WW DOMAIN'''<br /> | ||
==Overview== | ==Overview== | ||
Two new NMR structures of WW domains, the mouse formin binding protein and | 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== | ==About this Structure== | ||
1E0M is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | 1E0M is a [http://en.wikipedia.org/wiki/Protein_complex 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]. | ||
==Reference== | ==Reference== | ||
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[[Category: Civera, C.]] | [[Category: Civera, C.]] | ||
[[Category: Gervais, V.]] | [[Category: Gervais, V.]] | ||
[[Category: Macias, M | [[Category: Macias, M J.]] | ||
[[Category: Oschkinat, H.]] | [[Category: Oschkinat, H.]] | ||
[[Category: protein design]] | [[Category: protein design]] | ||
[[Category: wwprototype]] | [[Category: wwprototype]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:22:28 2008'' | ||
Revision as of 13:22, 21 February 2008
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PROTOTYPE WW DOMAIN
OverviewOverview
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 StructureAbout this Structure
1E0M is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
ReferenceReference
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 [[Category: ]]
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