Crystal Structure of the TSP-1 Type 1 Repeats: A Novel Layered Fold and Its Biological Implication

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, antiparall...

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Veröffentlicht in:The Journal of cell biology 2002-10, Vol.159 (2), p.373-382
Hauptverfasser: Tan, Kemin, Duquette, Mark, Liu, Jin-huan, Dong, Yicheng, Zhang, Rongguang, Joachimiak, Andrzej, Lawler, Jack, Wang, Jia-huai
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Sprache:eng
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Zusammenfassung: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.
ISSN:0021-9525
1540-8140
DOI:10.1083/jcb.200206062