1e0m
From Proteopedia
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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
1E0M is a Protein complex structure of sequences from [1]. 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 [[Category: ]]
Page seeded by OCA on Sun Nov 25 03:54:42 2007
