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

Structure study of osteostatin PTHrP[Thr107](107-139).

The structure of chicken osteostatin or parathyroid hormone-related protein (PTHrP) (residues 107-139) containing an Ala/Thr substitution at the N-terminus was studied using two-dimensional proton NMR spectroscopy in an aqueous environment. Osteostatin is a separate circulating domain responsible for a range of activities related to the modulation of bone formation as well as keratinocyte proliferation. Anti-mitogenic properties of osteostatin have been detected in breast cancer cells and cytosolic calcium is used by osteostatin to signal in some neurons through a non-PTH receptor, unlike the separate circulating N-terminal domain. A structural basis for the activity is presented with particular emphasis given to the conformation of the bioactive segment 107-111, forming part of a finger-like projection capable of binding to the non-PTH receptor both in the presence and absence of the remainder of the molecule which appears simply to act as a largely globular carrier.[1]

References

  1. Structure study of osteostatin PTHrP[Thr107](107-139). Cuthbertson, R.M., Kemp, B.E., Barden, J.A. Biochim. Biophys. Acta (1999) [Pubmed]
 
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