A. Kristina Downing

TL;DR: The solution structure of the SH3 domain of the 85 kd regulatory subunit of phosphatidylinositol 3-kinase is shown to be a compact beta barrel consisting of five beta strands arranged in two beta sheets of three and two strands, similar to that of chicken brain alpha spectrin but represents a distinct class of SH3domain.

TL;DR: Intramolecular disulfide bonding, solution structure, and dynamics of a prototypical chordin-like CR repeat from procollagen IIA (CRColIIA), which has been previously shown to bind TGF-β1 and bone morphogenetic protein-2 are described.

TL;DR: The solution structure of the PH domain of the GTPase dynamin, one of a number of proteins that have PH domains and interact with GTP, is determined and shows that, despite the low level of sequence similarity between different PH domains, they do have a characteristic polypeptide fold.

TL;DR: The data demonstrate that calcium plays a key role in stabilising the rigidity of the domain pair on the pico- to millisecond time-scale and provide important insight into the properties of intact fibrillin-1, the consequences of Marfan syndrome causing mutations, and the ultrastructure of fibrillins and other extracellular matrix proteins.

TL;DR: The structural consequences of the N2144S amino acid change for the folding and calcium binding properties of mutant and wild-type TB6-cbEGF 32 and cbEGF32-33 domain pairs have been analysed by nuclear magnetic resonance and suggest that the TB 6-cb EGF32 linkage is flexible and the structural effect is localised to the interdomain linkage.