This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1e0l
From Proteopedia
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
