Title : Crystal structure of
the TSP-1 type 1 repeats: a novel layered fold and its biological implication
Abstract :
- Thrombospondin-1 ( TSP-1 ) contains three type 1 repeats (TSRs), which mediate cell attachment, glycosaminoglycan binding , inhibition of angiogenesis, activation of TGFbeta , and inhibition of matrix metalloproteinases
- The crystal structure of the TSRs reported in this article reveals a novel, antiparallel, three-stranded fold that consists of alternating stacked layers of tryptophan and arginine residues from respective strands, capped by disulfide bonds on each end
- The front face of the TSR contains a right-handed spiral, positively charged groove that might be the "recognition" face , mediating interactions with various ligands
- This is the first high-resolution crystal structure of a TSR domain that provides a prototypic architecture for structural and functional exploration of the diverse members of the TSR superfamily