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Originally published In Press as doi:10.1074/jbc.M003869200 on June 15, 2000

J. Biol. Chem., Vol. 275, Issue 35, 27284-27290, September 1, 2000
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Structure of Tuberoinfundibular Peptide of 39 Residues*

Andrea PiserchioDagger , Ted Usdin§, and Dale F. MierkeDagger ||

From the Dagger  Department of Chemistry, Brown University, Providence, Rhode Island 02912, the § Unit on Cell Biology, Laboratory of Genetics, National Institutes of Mental Health, Bethesda, Maryland 20892, and the  Department of Molecular Pharmacology, Physiology, and Biotechnology, Division of Biology and Medicine, Brown University, Providence, Rhode Island 02912

The recently identified natural peptide ligand, tuberoinfundibular peptide of 39 residues (TIP39) for the parathyroid hormone-2 (PTH2) receptor has been structurally characterized by high resolution NMR, circular dichroism, and computer simulations. The structural features of TIP39, determined in the presence of a zwitterionic lipid to mimic the membrane environment of the G-protein-coupled PTH2 receptor, consist of two alpha -helices, Ala5-Arg21 and Leu26-Val35. Although TIP39 shares limited sequence homology with parathyroid hormone (PTH), a comparison of the structural features of TIP39 and PTH illustrates a similar topological display of residues of the N-terminal helix important for PTH2 receptor activation. The C-terminal helix of TIP39 differs from that of PTH with respect to size and amphipathicity, suggesting an altered mode of binding for TIP39, consistent with the receptor chimera and ligand truncation studies presented in the accompanying paper (Hoare, S. R. J., Clark, J. A., and Usdin, T. B. (2000) J. Biol. Chem. 275, 27274-27283). The structural characterization of TIP39 also provides some insight into the lack of affinity of this novel ligand for the PTH1 receptor.

* This work was supported in part by National Institutes of Health (NIH) Grant GM54082, by the Research Corporation through a Cottrell Scholar Award, and by a grant from the Dreyfus Foundation (to D. F. M.). Use of the 750-MHz instrument was supported through NIH Grant RR-00995.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| To whom correspondence should be addressed: Dept. of Molecular Pharmacology, Division of Biology and Medicine, Box G-B4, Brown University, Providence, RI 02912. Tel.: 401-863-1596; Fax: 401-863-1595; E-mail: dale_mierke@brown.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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