1e0l
From Proteopedia
(New page: 200px<br /><applet load="1e0l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e0l" /> '''FBP28WW DOMAIN FROM MUS MUSCULUS'''<br /> =...) |
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| - | [[Image:1e0l.gif|left|200px]]<br /><applet load="1e0l" size=" | + | [[Image:1e0l.gif|left|200px]]<br /><applet load="1e0l" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1e0l" /> | caption="1e0l" /> | ||
'''FBP28WW DOMAIN FROM MUS MUSCULUS'''<br /> | '''FBP28WW DOMAIN FROM MUS MUSCULUS'''<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== | ||
| - | 1E0L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 1E0L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E0L 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: fbp28]] | [[Category: fbp28]] | ||
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[[Category: ww domain]] | [[Category: ww domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:22:33 2008'' |
Revision as of 10:22, 21 February 2008
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FBP28WW DOMAIN FROM MUS MUSCULUS
Overview
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
1E0L is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 12:22:33 2008
