1e0l: Difference between revisions
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'''FBP28WW DOMAIN FROM MUS MUSCULUS''' | '''FBP28WW DOMAIN FROM MUS MUSCULUS''' | ||
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[[Category: Macias, M J.]] | [[Category: Macias, M J.]] | ||
[[Category: Oschkinat, H.]] | [[Category: Oschkinat, H.]] | ||
[[Category: | [[Category: Fbp28]] | ||
[[Category: | [[Category: Signal transduction]] | ||
[[Category: | [[Category: Ww domain]] | ||
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Revision as of 11:30, 2 May 2008
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 Fri May 2 14:30:42 2008
