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
Output (sent_index, trigger,
protein,
sugar,
site):
- 1. TGFbeta, , TGFbeta, glycosaminoglycan binding, -
- 1. contains, , TSP, three type 1 repeats, -
- 1. contains, , Thrombospondin-1, three type 1 repeats, -
- 1. metalloproteinases, , metalloproteinases, glycosaminoglycan binding, -
Output(Part-Of) (sent_index,
protein,
site):
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):