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1e0m

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[[Image:1e0m.gif|left|200px]]
[[Image:1e0m.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1e0m", creates the "Structure Box" on the page.
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{{STRUCTURE_1e0m| PDB=1e0m | SCENE= }}
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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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'''PROTOTYPE WW DOMAIN'''
'''PROTOTYPE WW DOMAIN'''
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==About this Structure==
==About this Structure==
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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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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://www.ncbi.nlm.nih.gov/pubmed/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]
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[[Category: ]]
 
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[[Category: Protein complex]]
 
[[Category: Civera, C.]]
[[Category: Civera, C.]]
[[Category: Gervais, V.]]
[[Category: Gervais, V.]]
[[Category: Macias, M J.]]
[[Category: Macias, M J.]]
[[Category: Oschkinat, H.]]
[[Category: Oschkinat, H.]]
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[[Category: protein design]]
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[[Category: Protein design]]
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[[Category: wwprototype]]
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[[Category: Wwprototype]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:30:45 2008''
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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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Revision as of 11:30, 2 May 2008

Template:STRUCTURE 1e0m

PROTOTYPE WW DOMAIN


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

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 Fri May 2 14:30:45 2008

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