0000000000236096
AUTHOR
Diane E. Zimmerman
High-resolution solution NMR structure of the Z domain of staphylococcal protein A
Staphylococcal protein A (SpA) is a cell-wall-bound pathogenicity factor from the bacterium Staphylococcus aureus. Because of their small size and immunoglobulin (IgG)-binding activities, domains of protein A are targets for protein engineering efforts and for the development of computational approaches for de novo protein folding. The NMR solution structure of an engineered IgG-binding domain of SpA, the Z domain (an analog of the B domain of SpA), has been determined by simulated annealing with restrained molecular dynamics on the basis of 671 conformational constraints. The Z domain contains three well-defined alpha-helices corresponding to polypeptide segments Lys7 to Leu17 (helix 1), G…
A novel RNA-binding motif in influenza A virus non-structural protein 1.
The solution NMR structure of the RNA-binding domain from influenza virus non-structural protein 1 exhibits a novel dimeric six-helical protein fold. Distributions of basic residues and conserved salt bridges of dimeric NS1(1-73) suggest that the face containing antiparallel helices 2 and 2′ forms a novel arginine-rich nucleic acid binding motif.
High Resolution Solution NMR Structure of the Z Domain of Staphylococcal Protein A. Analysis of Secondary Structure for Free Z Domain and Bounded to IgG Antibody
Staphylococcal protein A (SpA) is a cell-wall-bound pathogenicity factor from the bacterium Staphylcoccus aureus. It exhibits tight binding to many IgG, IgA and IgM molecules at site(s) different from antigen-combining site. Because of their small size and immunoglobulin (IgG)-binding activities, domains of protein A are important targets for protein engineering efforts and for the development of computational approaches for de novo protein folding.