Richard A. Kammerer

TL;DR: The crystal structure of a parallel pentameric coiled coil, constituting the oligomerization domain in the cartilage oligomeric matrix protein (COMP), was determined at 2.05 angstroms resolution and has marked similarities with proposed models of thepentameric transmembrane ion channels in phospholamban and the acetylcholine receptor.

TL;DR: By replacing the N-terminal portion of Ang1 with the short coiled-coil domain of cartilage oligomeric matrix protein (COMP), this variant is a soluble, stable, and potent Ang1 variant, COMP-Ang1, which is more potent than native Ang1 in phosphorylating the tyrosine kinase with Ig and epidermal growth factor homology domain 2 (Tie2) receptor and Akt in primary cultured endothelial cells.

TL;DR: A method to stabilize collagen-like peptides by fusing them to the N terminus of the bacteriophage T4 fibritin foldon domain is reported, and it is shown that the foldondomain, which comprises only 27 amino acid residues, forms an obligatory trimer with a high degree of thermal stability.

TL;DR: Structural analysis of a complex of tubulin and tubulin tyrosine ligase (TTL) reveals insights into TTL’s enzymatic mechanism, how it discriminates between α- and β-tubulin, and its possible evolutionary origin.

TL;DR: A 13-residue sequence pattern that occurs with limited sequence variations in many two-stranded coiled coils and that is absolutely required for the assembly of the Dictyostelium discoideum actin-bundling protein cortexillin I and the yeast transcriptional activator GCN4 is reported.