1e0m: Difference between revisions

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[[Image:1e0m.gif|left|200px]]<br /><applet load="1e0m" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1e0m.gif|left|200px]]
caption="1e0m" />
 
'''PROTOTYPE WW DOMAIN'''<br />
{{Structure
|PDB= 1e0m |SIZE=350|CAPTION= <scene name='initialview01'>1e0m</scene>
|SITE=  
|LIGAND=  
|ACTIVITY=  
|GENE=  
}}
 
'''PROTOTYPE WW DOMAIN'''
 


==Overview==
==Overview==
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==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://oca.weizmann.ac.il/oca-bin/ocashort?id=1E0M OCA].  
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].  


==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10802733 10802733]
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]
[[Category: ]]
[[Category: ]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: wwprototype]]
[[Category: wwprototype]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:22:28 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:47:31 2008''

Revision as of 11:47, 20 March 2008

File:1e0m.gif


PDB ID 1e0m

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Coordinates: save as pdb, mmCIF, xml



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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