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Published online 21 October 2002. doi:10.1083/jcb.200206062
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© The Rockefeller University Press, 0021-9525/2002/10/373 $5.00
The Journal of Cell Biology, Volume 159, Number 2, 373-382

Article

Crystal structure of the TSP-1 type 1 repeats

: a novel layered fold and its biological implication



Kemin Tan1,3, Mark Duquette2,4, Jin-huan Liu1,3, Yicheng Dong1,3, Rongguang Zhang7, Andrzej Joachimiak7, Jack Lawler2,4 and Jia-huai Wang1,5,6

1 Dana-Farber Cancer Institute, Boston, MA 02115
2 Beth Israel Deaconess Medical Center, Boston, MA 02215
3 Departments of Medicine, Harvard Medical School, Boston, MA 02115
4 Pathology, Harvard Medical School, Boston, MA 02115
5 Pediatrics, Harvard Medical School, Boston, MA 02115
6 Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115
7 Biosciences Division, Argonne National Laboratories, Argonne, IL 60439

Address correspondence to Jia-huai Wang, Dana-Farber Cancer Institute, Harvard Medical School, 44 Binney St., Room SM-1036, Boston, MA 02115. Tel.: (617) 632-3983. Fax: (617) 632-4393. E-mail: jwang{at}red.dfci.harvard.edu; or Jack Lawler, Beth Israel Deaconess Medical Center, Harvard Medical School, 99 Brookline Ave., Boston, MA 02215. Tel.: (617) 667-1694. Fax: (617) 667-3591. E-mail: lawler{at}mbcrr.harvard.edu

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

Key Words: thrombospondin; TSR domain; X-ray structure; angiogenesis; GAG binding


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