Structural features of parathyroid hormone receptor coupled to GαS-protein

Biophysical Journal

Volumn 92, Issue 2, 2007, Pages 535-540

  Plati, Jessica ^a   Tsomaia, Natia ^b   Piserchio, Andrea ^b,c   Mierke, Dale F ^a,b  

^a BROWN UNIVERSITY   (United States)

^b BROWN UNIVERSITY   (United States)

^c NEW YORK STRUCTURAL BIOLOGY CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; G PROTEIN COUPLED RECEPTOR; GUANINE NUCLEOTIDE BINDING PROTEIN; PARATHYROID HORMONE RECEPTOR; PLASMID VECTOR;

ARTICLE; MOLECULAR DYNAMICS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR OVERHAUSER EFFECT; PROTEIN INTERACTION; STRUCTURE ANALYSIS;

EID: 33846454003     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.094813     Document Type: Article

References (39)

1. Dempster, D. W., F. Cosman, M. Parisien, V. Shen, and R. Lindsay. 1993. Anabolic actions of parathyroid hormone on bone. Endocr. Rev. 14:690-709.
2. Chorev, M., and M. Rosenblatt. 1994. Structure function analysis of parathyroid hormone and parathyroid hormone-related protein. In The Parathyroids. J.P. Bilezikian, M. A. Levine, and R. Marcus, editors. Raven Press, New York. 139-156.
3. Abou-Samra, A.-B., H. Jüppner, T. Force, M. W. Freeman, X. F. Kong, E. Schipani, P. Urena, J. Richards, J. V. Bonventre, J. T. Potts, Jr., H. Kronenberg, and G. V. Segre. 1992. Expression cloning of a common receptor for parathyroid hormone and parathyroid hormone-related peptide from rat osteoblast-like cells: a single receptor stimulates intracellular accumulation of both cAMP and inositol trisphosphates and increases intracellular free calcium. Proc. Natl. Acad. Sci. USA. 89:2732-2736.
4. Civitelli, R., T. J. Martin, A. Fausto, S. L. Gunsten, K. A. Hruska, and L. V. Avioli. 1989. Parathyroid hormone-related peptide transiently increases cytosolic calcium in osteoblast-like cells: comparison with parathyroid hormone. Endocrinology. 125:1204-1210.
5. 2+ signaling by the recombinant human PTH/PTHrP receptor stably expressed in a human kidney cell line. Bone. 18:381-389.
6. Hedin, K. E., K. Duerson, and D. E. Clapham. 1993. Specificity of receptor-G protein interactions: Searching for the structure behind the signal. Cell. Signal. 5:505-518.
7. Savarese, T. M., and C. M. Fraser. 1992. In vitro mutagenesis and the search for structure-function relationships among G protein-coupled receptors. Biochem. J. 283:1-19.
8. Conklin, B. R., and H. R. Bourne. 1993. Structural elements of Gα subunits that interact with Gβγ, receptors, and effectors. Cell. 73:631-641.
9. Spiegel, A. M., W. F. Simonds, T. L. Jones, P. K. Goldsmith, and C. G. Unson. 1990. Biochem. Soc. Symp. 56:61-69.
10. s carboxyl-terminal decapeptide. FEBS Lett. 249:189-194.
11. Pantaloni, C., and Y. Audigier. 1993. Functional domains of the Gs alpha subunit: role of the C-terminus in the receptor-dependent and receptor-independent activation. J. Recept. Res. 13:591-608.
12. Schwindinger, W. F. 1994. A novel Gsa mutant in a patient with Albright hereditary osteodystrophy uncouples cell surface receptors from adenylyl cyclase. J. Biol. Chem. 269:25387-25391.
13. Sullivan, K. A., R. T. Miller, S. B. Masters, B. Beiderman, W. Heideman, and H. R. Bourne. 1987. Identification of receptor contact site involved in receptor-G protein coupling. Nature. 330:758-760.
14. Rall, T., and B. A. Harris. 1987. Identification of the lesion in the stimulatory GTP-binding protein of the uncoupled S49 lymphoma. FEBS Lett. 224:365-371.
15. Reference deleted in proof.
16. s. A cause of Pseudohypoparathyroidism type Ib. J. Biol. Chem. 276:165-171.
17. sα that alter the fidelity of receptor activation. Mol. Pharmacol. 50:885-890.
18. α16 contribute to the specificity of activation by the C5a receptor. Mol. Pharmacol. 47:218-223.
19. sα in which substitutions decrease receptor-mediated activation and increase receptor affinity. Mol. Pharmacol. 57:1081-1092.
20. αβγ binding surfaces support a model of the G-protein-receptor complex. Proc. Natl. Acad. Sci. USA. 93:7507-7511.
21. Strader, C. D., T. M. Fong, M. R. Tota, D. Underwood, and R. A. F. Dixon. 1994. Structure and function of G protein-coupled receptors. Annu. Rev. Biochem. 63:101-132.
22. Komatsu, Y., and G. V. Segre. 1998. Interactions between the intracellular domains of the PTH/PTHrP receptor and trimeric G proteins. In American Society for Bone and Mineral Research. Elsevier, San Francisco. S253.
23. Pellegrini, M., M. Royo, M. Chorev, and D. F. Mierke. 1996. Conformational characterization of a peptide mimetic of the third cytoplasmic loop of the G-protein coupled parathyroid hormone/parathyroid hormone related protein receptor. Biopolymers. 40:653-666.
24. Mierke, D. F., M. Royo, M. Pellegrini, H. Sun, and M. Chorev. 1996. Peptide mimetic of the third cytoplasmic loop of the PTH/PTHrP receptor. J. Am. Chem. Soc. 118:8998-9004.
25. Mayer, M., and B. Meyer. 2000. Mapping the active site of angiotensin-converting enzyme by transferred NOE spectroscopy. J. Med. Chem. 43:2093-2099.
26. Haselhorst, T., J. F. Espinosa, J. Jimenez-Barbero, T. Sokolowski, P. Kosma, H. Brade, L. Brade, and T. Peters. 1999. NMR experiments reveal distinct antibody-bound conformations of a synthetic disaccharide representing a general structural element of bacterial lipopolysaccharide epitopes. Biochemistry. 38:6449-6459.
27. Meyer, B., T. Weimar, and T. Peters. 1997. Screening mixtures for biological activity by NMR. Eur. J. Biomchem. 246:705-709.
28. αi1-bound structures of IC3 and a mutant with altered G-protein specificity. Protien Sci. 11:2526-2531.
29. Lindahl, E., B. Hess, and D. van der Spoel. 2001. GROMACS 3.0: a package for molecular simulation and trajectory analysis. J. Mol. Mod. 7:306-317.
30. Berendsen, H. J. C., D. van der Spoel, and R. van Drunen. 1995. GROMACS: a message-passing parallel molecular dynamics implementation. Comp. Phys. Comm. 91:43-56.
31. Mayer, M., and B. Meyer. 1999. Characterization of ligand binding by saturation transfer difference NMR spectroscopy. Angew. Chem. Int. Ed. Engl. 38:1784-1788.
32. Mayer, M., and B. Meyer. 2001. Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor. J. Am. Chem. Soc. 123:6108-6117.
33. sα. Science. 278:1943-1947.
34. Liu, J., N. Blin, B. R. Conklin, and J. Wess. 1996. Molecular mechanisms involved in muscarinic acetylcholine receptor-mediated G-protein activation studied by insertion mutagenesis. J. Biol. Chem. 271:6172-6178.
35. Kosugi, S., F. Okajima, T. Ban, A. Hidaka, A. Shenker, and L. D. Kohn. 1992. Mutation of alanine 623 in the third cytoplasmic loop of the rat thyrotropin (TSH) receptor results in a loss in the phosphoinositide but not cAMP signal induced by TSH and receptor autoantibodies. J. Biol. Chem. 267:24153-24156.
36. Cotecchia, S., S. Exum, M. G. Caron, and R. J. Lefkowitz. 1990. Regions of the 1-adrenergic receptor involved in coupling to phosphatidylinositol hydrolysis and enhanced sensitivity of biological function. Proc. Natl. Acad. Sci. USA. 87:2896-2900.
37. Högger, P., M. S. Shockley, J. Lameh, and W. Sadee. 1995. Activating and inactivating mutations in N- and C-terminal i3 loop junctions of muscarinic acetylcholine Hm1 receptors. J. Biol. Chem. 270:7405-7410.
38. s. Requirement for multiple cytoplasmic domains in the coupling process. J. Biol. Chem. 266:4816-4821.
39. q/11 by the m3 muscarinic acetylcholine receptor. J. Biol. Chem. 270:17741-17748.