Structural Analysis of Ww Domains and Design of a Ww Prototype

摘要: Two new NMR structures of WW domains, the mouse formin binding protein and a putative 84.5 kDa from Saccharomyces cerevisiae, show that this domain, only 35 amino acids in length, defines smallest monomeric triple-stranded antiparallel β-sheet domain is stable absence disulfide bonds, tightly bound ions or ligands. The structural roles conserved residues have been studied using site-directed mutagenesis both wild type domains. Crucial interactions responsible for stability structure identified. Based on network highly long range across supports fold systematic analysis family, we designed folded prototype sequence.