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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Structure of the calcium-rich signature domain of human thrombospondin-2.

Thrombospondins (THBSs) are secreted glycoproteins that have key roles in interactions between cells and the extracellular matrix. Here, we describe the 2.6-A-resolution crystal structure of the glycosylated signature domain of human THBS2, which includes three epidermal growth factor-like modules, 13 aspartate-rich repeats and a lectin-like module. These elements interact extensively to form three structural regions termed the stalk, wire and globe. The THBS2 signature domain is stabilized by these interactions and by a network of 30 bound Ca(2+) ions and 18 disulfide bonds. The structure suggests how genetic alterations of THBSs result in disease.[1]

References

  1. Structure of the calcium-rich signature domain of human thrombospondin-2. Carlson, C.B., Bernstein, D.A., Annis, D.S., Misenheimer, T.M., Hannah, B.L., Mosher, D.F., Keck, J.L. Nat. Struct. Mol. Biol. (2005) [Pubmed]
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