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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.

SUBMITTER: Tan K

PROVIDER: S-EPMC2173040 | biostudies-literature | 2002 Oct

REPOSITORIES: biostudies-literature

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Crystal structure of the TSP-1 type 1 repeats: a novel layered fold and its biological implication.

Tan Kemin K Duquette Mark M Liu Jin-huan JH Dong Yicheng Y Zhang Rongguang R Joachimiak Andrzej A Lawler Jack J Wang Jia-huai JH

The Journal of cell biology 20021021 2

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 con ...[more]

PMID: 12391027

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