Crystal structure of the TSP-1 type 1 repeats

Author:

Tan Kemin12,Duquette Mark34,Liu Jin-huan12,Dong Yicheng12,Zhang Rongguang5,Joachimiak Andrzej5,Lawler Jack34,Wang Jia-huai167

Affiliation:

1. Dana-Farber Cancer Institute, Boston, MA 02115

2. Departments of Medicine, Harvard Medical School, Boston, MA 02115

3. Beth Israel Deaconess Medical Center, Boston, MA 02215

4. Pathology, Harvard Medical School, Boston, MA 02115

5. Biosciences Division, Argonne National Laboratories, Argonne, IL 60439

6. Pediatrics, Harvard Medical School, Boston, MA 02115

7. Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115

Abstract

Thrombospondin-1 (TSP-1) contains three type 1 repeats (TSRs), which mediate cell attachment, glycosaminoglycan binding, inhibition of angiogenesis, activation of TGFβ, 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.

Publisher

Rockefeller University Press

Subject

Cell Biology

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