title: 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.
authors.affiliation: Dana-Farber Cancer Institute, Harvard Medical School, 44 Binney Street, Boston, MA 02115, USA.
authors.forename: Kemin
authors.initials: K
authors.lastname: Tan
authors.forename: Mark
authors.initials: M
authors.lastname: Duquette
authors.forename: Jin-huan
authors.initials: JH
authors.lastname: Liu
authors.forename: Yicheng
authors.initials: Y
authors.lastname: Dong
authors.forename: Rongguang
authors.initials: R
authors.lastname: Zhang
authors.forename: Andrzej
authors.initials: A
authors.lastname: Joachimiak
authors.forename: Jack
authors.initials: J
authors.lastname: Lawler
authors.forename: Jia-huai
authors.initials: JH
authors.lastname: Wang
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D018360:Crystallography, X-Ray; D006801:Humans; D008969:Molecular Sequence Data; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D013329:Structure-Activity Relationship; D019700:Thrombospondin 1 / Q000737:chemistry*
chemical_list: D019700:Thrombospondin 1