Journal
JOURNAL OF CELL BIOLOGY
Volume 159, Issue 2, Pages 373-382Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200206062
Keywords
thrombospondin; TSR domain; X-ray structure; angiogenesis; GAG binding
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Funding
- NCI NIH HHS [CA 92644, P01 CA092644] Funding Source: Medline
- NHLBI NIH HHS [HL 49081, R01 HL068003, R01 HL049081, HL 68003] Funding Source: Medline
- NIGMS NIH HHS [GM 56008] Funding Source: Medline
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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.
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