Static and dynamic roles of extracellular loops in G-protein-coupled receptors: A mechanism for sequential binding of thyrotropin-releasing hormone to its receptor

Biophysical Journal

Volumn 74, Issue 3, 1998, Pages 1087-1100

  Colson, Anny Odile ^a   Perlman, Jeffrey H ^b   Smolyar, Alex ^a   Gershengorn, Marvin C ^b   Osman, Roman ^a  

^a MOUNT SINAI SCHOOL OF MEDICINE   (United States)

^b WEILL CORNELL MEDICAL COLLEGE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; PROTIRELIN; PROTIRELIN RECEPTOR; RECEPTOR PROTEIN;

ANIMAL CELL; ARTICLE; HORMONE RECEPTOR INTERACTION; LIGAND BINDING; MOLECULAR DYNAMICS; MONKEY; NONHUMAN; PROTEIN DOMAIN; PROTEIN FAMILY; SIMULATION;

EID: 0031909269     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)77827-0     Document Type: Article

References (42)

1. Amadei, A., B. M. Linssen, and H. J. C. Berendsen. 1993. Essential dynamics of proteins. Proteins. 17:412-425.
2. Baldwin, J. M. 1993. The probable arrangement of the helices in G protein-coupled receptors. EMBO J. 12:1693-1703.
3. Ballesteros, J. A., and H. Weinstein. 1995. Integrated methods for the construction of three-dimensional models and computational probing of structure-function relations in G-protein-coupled receptors. In Receptor Molecular Biology. Academic Press, New York. 366-428.
4. Brooks, B., and M. Karplus. 1983a. Harmonic dynamics of proteins: normal modes and fluctuations in bovine pancreatic trypsin inhibitor. Proc. Natl. Acad. Sci. USA. 80:6571-6575.
5. Brooks, B. R., R. E. Bruccoleri, B. D. Olafson, D. J. States, S. Swaminathan, and M. Karplus. 1983b. CHARMM: a program for macromolecular energy, minimization and dynamics calculations. J. Comp. Chem. 4:187-217.
6. Colson, A. O., J. H. Perlman, R. Jain, L. A. Cohen, R. Osman, and M. C. Gershengorn. 1997. Sequential binding of TRH to the TRH receptor: a model for small ligand binding to G-protein coupled receptors. Biophys. J. 72:A122.
7. 2 receptor. Proc. Natl. Acad. Sci. USA. 88:8111-8115.
8. Feher, V. A., E. P. Baldwin, and F. W. Dahlquist. 1996. Access of ligands to cavities within the core of a protein is rapid. Nature Struct. Biol. 3:516-521.
9. Findlay, J., and E. Eliopoulos. 1990. Three-dimensional modelling of G protein-linked receptors. Trends Pharmacol. Sci. 11:492-499.
10. Garcia, K. C., P. M. Ronco, P. J. Verroust, A. T. Brünger, and L. M. Amzel. 1992. Three-dimensional structure of an angiotensin II-fab complex at 3 Å: hormone recognition by an anti-idiotypic antibody. Science. 257:502-507.
11. Gershengorn, M. C., and R. Osman. 1996. Molecular and cellular biology of thyrotropin releasing hormone receptors. Physiol. Rev. 76:175-191.
12. Gershengorn, M. C., and C. N. Thaw. 1991. Regulation of thyrotropin-releasing hormone receptors is cell type specific: comparison of endogenous pituitary receptors and receptors transfected into non-pituitary cells. Endocrinology. 128:1204-1206.
13. Go, N., T. Noguti, and T. Nishikawa. 1983. Dynamics oa a small globular protein in terms of low-frequency vibrational modes. Proc. Natl. Acad. Sci. USA. 80:3696-3700.
14. Han, B., and A. H. Tashjian. 1995a. Importance of extracellular domains for ligand binding in the thyrotropin releasing hormone receptor. Mol. Endocrinol. 9:1708-1719.
15. Han, B., and A. H. Tashjian. 1995b. Identification of Asn289 as a ligand binding site in the rat thyrotropin releasing hormone (TRH) receptor as determined by complementary modifications in the ligand and receptor: a new model for TRH binding. Biochemistry. 34:13412-13422.
16. Horiuchi, T., and N. Go. 1991. Projection of Monte Carlo and molecular dynamics trajectories onto the normal mode axes: human lysozyme. Proteins. 10:106-116.
17. Ichiye, T., and M. Karplus. 1991. Collective motions in proteins: a covariance analysis of atomic fluctuations in molecular dynamics and normal mode simulations. Proteins. 11:205-217.
18. Kyle, D. J., S. Chakravarty, J. A. Sinsko, and T. M. Stormann. 1994. A proposed model of bradykinin bound to the rat B2 receptor and its utility for drug design. J. Med. Chem. 37:1347-1354.
19. Laakkonen, L. J., F. Guarnieri, J. H. Perlman, M. C. Gershengorn, and R. Osman. 1996. A refined model of the thyrotropin releasing hormone (TH) receptor binding pocket: novel mixed mode Monte Carlo/ stochastic dynamics simulations of the complex between TRH and TRH receptor. Biochemistry. 35:7651-7663.
20. Laskowski, R. A., M. W. MacArthur, D. S. Moss, and J. M. Thornton. 1993. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26:283-291.
21. 2 adrenergic receptor protein based on computer modeling studies. J. Mol. Biol. 225:859-871.
22. McGregor, M. J., S. A. Islam, and M. J. E. Sternberg. 1987. Analysis of the relationship between side-chain conformation and secondary structure in globular proteins. J. Mol. Biol. 198:295-310.
23. Morris, A. L., M. W. MacArthur, E. G. Hutchinson, and J. M. Thornton. 1992. Stereochemical quality of protein structure coordinates. Proteins. 12-345-364.
24. Nicholls, A. 1992. GRASP: graphical representation and analysis of surface properties. Columbia University, New York.
25. Perlman, J. H., A. D. Colson, R. Jain, B. Czyzewski, L. A. Cohen, R. Osman, and M. C. Gershengorm. 1998. Role of the extracellular loops of the thyrotropin-releasing hormone (TRH) receptor. Evidence for an initial interaction with TRH. Biochemistry. In press.
26. Perlman, J. H., O. Colson, W. Wang, K. Bence, R. Osman, and M. C. Gersherngorn. 1997. Interactions between conserved residues in transmembrane helices 1, 2 and 7 of the thyrotropin-releasing hormone receptor. J. Biol. Chem. 272:11937-11942.
27. Perlman, J. H., L. Laakkonen, R. Osman, and M. C. Gershengorn. 1994a. A model of thyrotropin-releasing hormone (TRH) receptor binding pocket: evidence for a second direct interaction between transmembrane helix 3 and TRH. J. Biol. Chem. 269:23383-23386.
28. Perlman, J. H., L. Laakkonen, R. Osman, and M. C. Gershengorn. 1995a. Distinct roles for arginines in transmembrane helices 6 and 7 of the thyrotropin-releasing hormone receptor. Mol. Pharmacol. 47:480-484.
29. Perlman, J. H., L. J. Laakkonen, F. Guarnieri, R. Osman, and M. C. Gershengorn. 1996. A refined model of the thyrotropin releasing hormone (TRH) receptor binding pocket: experimental analysis and energy minimization of the complex between TRH and TRH receptor. Biochemistry. 35:7643-7650.
30. Perlman, J. H., D. R. Nussenzveig, R. Osman, and M. C. Gershengorn. 1992. Thyrotropin-releasing hormone binding to the mouse pituitary receptors does not involve ionic interactions: a mode for neutral peptide binding to G protein-coupled receptors. J. Biol. Chem. 267: 24413-24417.
31. Perlman, J. H., C. N. Thaw, L. Laakkonen, C. Y. Bowers, R. Osman, and M. C. Gershengorn. 1994b. Hydrogen bonding interaction of the thyrotropin-releasing hormone (TRH) with transmembrane tyrosine 106 of the TRHR receptor. J. Biol. Chem. 269:1610-1613.
32. Perlman, J. H. W. Wang, D. R. Nussenzveig, and M. C. Gershengorn. 1995b. A disulfide bond between conserved extracellular cysteines in the thyrotropin releasing hormone receptor is critical for binding. J. Biol. Chem. 270:24682-24685.
33. Rini, J. M., U. Schulze-Gahmen, and I. A. Wilson. 1992. Structural evidence for induced fit as a mechanism for antibody-antigen recognition. Science. 255:959-965.
34. Seno, Y., and N. Go. 1990a. Deoxymyoglobin studied by the conformational normal mode analysis. I. Dynamics of globin and the heme-globin interaction. J. Mol. Biol. 216:95-109.
35. Seno, Y., and N. Go. 1990b. Deoxymyoglobin studied by the conformational normal mode analysis. II. The conformational change upon oxygenation. J. Mol. Biol. 216:111-126.
36. Shenkin, P. S., and D. Q. McDonald. 1994. Cluster analysis of molecular conformations. J. Comp. Chem. 15:899.
37. Stanfield, R. L., and I. A. Wilson. 1995. Protein-peptide interactions. Curr. Opin. Struct. Biol. 5:103-113.
38. Straub, R. E., G. C. Frech, R. H. Joho, and M. C. Gershengorn. 1990. Expression cloning of cDNA encoding the mouse pituitary thyrotropin-releasing hormone receptor. Proc. Natl. Acad. Sci. USA. 87:9514-9518.
39. Sylte, I., O. Edvardsen, and S. G. Dahl. 1996. Molecular modeling of UH-301 and 5-HT1a receptor interactions. Protein Eng. 9:149-160.
40. Teeter, M. M., and D. A. Case. 1990. Harmonic and quasi-harmonic descriptions of crambin. J. Phys. Chem. 94:8091-8097.
41. van Aalten, D. M., F. A. Amadei, A. B. M. Linssen, V. G. H. Eijsink, G. Vriend, and H. J. C. Berendsen. 1995a. The essential dynamics of thermolysin: confirmation of the hinge bending motion and comparison of simulations in vacuum and water. Proteins. 22:45-54.
42. van Aalten, D. M. F., J. B. C. Findlay, A. Amadei, and H. J. C. Berendsen. 1995b. Essential dynamics of the cellular retinol binding protein: evidence for ligand induced conformational changes. Protein Eng. 8:1129-1135.