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Fragile X syndrome is the most common form of inherited mental retardation in humans, with an estimated prevalence of about 1 in 4000 males. Although several observations indicate that the absence of functional Fragile X Mental Retardation Protein (FMRP) is the underlying basis of Fragile X syndrome, the structure and function of FMRP are currently unknown. Here, we present an X-ray crystal structure...
The formation of amyloid fibers and their deposition in the body is a characteristic of a number of devastating human diseases. Here, we propose a structural model, based on X-ray diffraction data, for the basic structure of an amyloid fibril formed by using the variants of the B1 domain of IgG binding protein G of Streptococcus. The model for the fibril incorporates four β sheets in a bundle with...
The tetratricopeptide repeat (TPR) is a 34-amino acid α-helical motif that occurs in over 300 different proteins. In the different proteins, three to sixteen or more TPR motifs occur in tandem arrays and function to mediate protein-protein interactions. The binding specificity of each TPR protein is different, although the underlying structural motif is the same. Here we describe a statistical approach...
Background: Rop is an RNA binding, dimeric, four-helix bundle protein with a well-defined, regular hydrophobic core ideally suited for redesign studies. A family of Rop variants in which the hydrophobic core was systematically redesigned has previously been created and characterized.Results: We present a structural and thermodynamic analysis of Ala 2 Ile 2 -6, a variant of Rop with...
Background: Both backbone hydrogen bonding and interactions between sidechains stabilize β sheets. Cross-strand interactions are the closest contacts between the sidechains of a β sheet. Here we investigate the energetics of cross-strand interactions using a variant of the B1 domain of immunoglobulin G (IgG) binding protein G (β1) as our model system.Results: Pairwise mutations of polar and nonpolar...
There is a buzz of excitement and discussion in the protein folding and design community following the publication of papers by Stephen Mayo and colleagues, describing the implementation of their new computer-assisted strategy for protein design.
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