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Structure of the Calcium-Rich Signature Domain of Human Thrombospondin-2
Nature Structural & Molecular Biology (2005)
  • C. Britt Carlson, Parkland College
  • Douglas A Bernstein
  • Douglas S. Annis
  • Tina M. Misenheimer
  • Blue-leaf A. Hannah
  • Deane F. Mosher
  • James L. Keck
Thrombospondins (TSPs) are secreted glycoproteins that play key roles in interactions between cells and the extracellular matrix. Here, we describe the 2.6 Å resolution crystal structure of the glycosylated signature domain of human TSP-2, which includes three epidermal growth factor-like (EGF-like) modules, 13 aspartate-rich repeats, and a lectin-like module. These elements interact extensively to form three striking structural regions termed the stalk, wire, and globe. The TSP-2 signature domain is stabilized by these interactions and by a network of 30 bound Ca2+ ions and 18 disulfide bonds. The structure suggests how genetic alterations of TSPs result in disease.
Publication Date
October, 2005
Citation Information
C. Britt Carlson, Douglas A Bernstein, Douglas S. Annis, Tina M. Misenheimer, et al.. "Structure of the Calcium-Rich Signature Domain of Human Thrombospondin-2" Nature Structural & Molecular Biology Vol. 12 Iss. 10 (2005) p. 910 - 914 ISSN: 1545-9993 (Print); 1545-9985 (Online)
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