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Volumn 101, Issue 2, 2007, Pages 506-516

Topological analysis of the complex formed between neurokinin A and the NK2 tachykinin receptor

Author keywords

Fluorescence resonance energy transfer; G protein coupled receptor structure; Peptide conformation; Pharmacology

Indexed keywords

AMINO ACID; ENHANCED GREEN FLUORESCENT PROTEIN; NEUROKININ 2 RECEPTOR; NEUROKININ A; RHODOPSIN; TACHYKININ RECEPTOR;

EID: 34047120236     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2007.04473.x     Document Type: Article
Times cited : (9)

References (42)
  • 1
    • 0033845060 scopus 로고    scopus 로고
    • Different subtypes of tachykinin NK(1) receptor binding sites are present in the rat brain
    • Beaujouan J. C., Saffroy M., Torrens Y. and Glowinski J. (2000) Different subtypes of tachykinin NK(1) receptor binding sites are present in the rat brain. J. Neurochem. 75, 1015-1026.
    • (2000) J. Neurochem , vol.75 , pp. 1015-1026
    • Beaujouan, J.C.1    Saffroy, M.2    Torrens, Y.3    Glowinski, J.4
  • 2
    • 0027986888 scopus 로고
    • The ligand binding site of the neurokinin 2 receptor Site-directed mutagenesis and identification of neurokinin A binding residues in the human neurokinin 2 receptor
    • Bhogal N., Donnelly D. and Findlay J. B. (1994) The ligand binding site of the neurokinin 2 receptor Site-directed mutagenesis and identification of neurokinin A binding residues in the human neurokinin 2 receptor. J. Biol. Chem. 269, 27 269-27 274.
    • (1994) J. Biol. Chem , vol.269
    • Bhogal, N.1    Donnelly, D.2    Findlay, J.B.3
  • 3
    • 0027992225 scopus 로고
    • Synthesis and characterization of selective fluorescent ligands for the neurokinin NK2 receptor
    • Bradshaw C. G., Ceszkowski K., Turcatti G., Beresford I. J. and Chollet A. (1994) Synthesis and characterization of selective fluorescent ligands for the neurokinin NK2 receptor. J. Med. Chem. 37, 1991-1995.
    • (1994) J. Med. Chem , vol.37 , pp. 1991-1995
    • Bradshaw, C.G.1    Ceszkowski, K.2    Turcatti, G.3    Beresford, I.J.4    Chollet, A.5
  • 4
    • 0034548761 scopus 로고    scopus 로고
    • The common C-terminal sequences of substance P and neurokinin A contact the same region of the NK-1 receptor
    • Bremer A. A., Leeman S. E. and Boyd N. D. (2000) The common C-terminal sequences of substance P and neurokinin A contact the same region of the NK-1 receptor. FEBS Lett. 486, 43-48.
    • (2000) FEBS Lett , vol.486 , pp. 43-48
    • Bremer, A.A.1    Leeman, S.E.2    Boyd, N.D.3
  • 5
    • 0015861774 scopus 로고
    • Relationship between the inhibition constant (Ki) and the concentration of inhibitor which causes 50 per cent inhibition (IC50) of an enzymatic reaction
    • Cheng Y.-C. and Prussoff W. H. (1973) Relationship between the inhibition constant (Ki) and the concentration of inhibitor which causes 50 per cent inhibition (IC50) of an enzymatic reaction. Biochem. Pharmacol. 22, 3099-3108.
    • (1973) Biochem. Pharmacol , vol.22 , pp. 3099-3108
    • Cheng, Y.-C.1    Prussoff, W.H.2
  • 6
    • 0025630719 scopus 로고
    • Neurokinin A levels in the hypothalamus of rats and mice, effects of castration, gonadal steroids and expression of heterologous growth hormone genes
    • Debeljuk L., Ghosh P. and Bartke A. (1990) Neurokinin A levels in the hypothalamus of rats and mice, effects of castration, gonadal steroids and expression of heterologous growth hormone genes. Brain Res. Bull. 25, 717-721.
    • (1990) Brain Res. Bull , vol.25 , pp. 717-721
    • Debeljuk, L.1    Ghosh, P.2    Bartke, A.3
  • 8
    • 0032820766 scopus 로고    scopus 로고
    • The study of the conformation and interaction of two tachykinin peptides in membrane mimicking systems by NMR spectroscopy and pulsed field gradient diffusion
    • Gao X. and Wong T. C. (1999) The study of the conformation and interaction of two tachykinin peptides in membrane mimicking systems by NMR spectroscopy and pulsed field gradient diffusion. Biopolymers 50, 555-568.
    • (1999) Biopolymers , vol.50 , pp. 555-568
    • Gao, X.1    Wong, T.C.2
  • 9
    • 0033614975 scopus 로고    scopus 로고
    • Importance of the aromatic residue at position 6 of [Nle(10)]neurokinin A(4-10) for binding to the NK-2 receptor and receptor activation
    • Gembitsky D. S., Murnin M., Otvos F. L., Allen J., Murphy R. F. and Lovas S. (1999) Importance of the aromatic residue at position 6 of [Nle(10)]neurokinin A(4-10) for binding to the NK-2 receptor and receptor activation. J. Med. Chem. 42, 3004-3007.
    • (1999) J. Med. Chem , vol.42 , pp. 3004-3007
    • Gembitsky, D.S.1    Murnin, M.2    Otvos, F.L.3    Allen, J.4    Murphy, R.F.5    Lovas, S.6
  • 11
    • 0027402089 scopus 로고
    • Different binding epitopes on the NK1 receptor for substance P and non- peptide antagonist
    • Gether U., Johansen T. E., Snider R. M., Lowe J. A. d., Nakanishi S. and Schwartz T. W. (1993b) Different binding epitopes on the NK1 receptor for substance P and non- peptide antagonist. Nature 362, 345-348.
    • (1993) Nature , vol.362 , pp. 345-348
    • Gether, U.1    Johansen, T.E.2    Snider, R.M.3    Lowe, J.A.D.4    Nakanishi, S.5    Schwartz, T.W.6
  • 12
    • 0034014842 scopus 로고    scopus 로고
    • Molecular determinants of peptide and nonpeptide NK-2 receptor antagonists binding sites of the human tachykinin NK-2 receptor by site- directed mutagenesis
    • Giolitti A., Cucchi P., Renzetti A. R., Rotondaro L., Zappitelli S. and Maggi C. A. (2000) Molecular determinants of peptide and nonpeptide NK-2 receptor antagonists binding sites of the human tachykinin NK-2 receptor by site- directed mutagenesis. Neuropharmacology 39, 1422-1429.
    • (2000) Neuropharmacology , vol.39 , pp. 1422-1429
    • Giolitti, A.1    Cucchi, P.2    Renzetti, A.R.3    Rotondaro, L.4    Zappitelli, S.5    Maggi, C.A.6
  • 13
    • 0032977234 scopus 로고    scopus 로고
    • Is there a future for neuropeptide receptor ligands in the treatment of anxiety disorders?
    • Griebel G. (1999) Is there a future for neuropeptide receptor ligands in the treatment of anxiety disorders? Pharmacol. Ther. 82, 1-61.
    • (1999) Pharmacol. Ther , vol.82 , pp. 1-61
    • Griebel, G.1
  • 14
    • 0027673371 scopus 로고
    • A new approach to analysis and display of local lipophilicity/hydrophilicity mapped on molecular surfaces
    • Heiden W., Moeckel G. and Brickmann J. (1993) A new approach to analysis and display of local lipophilicity/hydrophilicity mapped on molecular surfaces. J. Comput. Aided Mol. Des. 7, 503-514.
    • (1993) J. Comput. Aided Mol. Des , vol.7 , pp. 503-514
    • Heiden, W.1    Moeckel, G.2    Brickmann, J.3
  • 15
    • 0030087710 scopus 로고    scopus 로고
    • Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer
    • Heim R. and Tsien R. Y. (1996) Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer. Curr. Biol. 6, 178-182.
    • (1996) Curr. Biol , vol.6 , pp. 178-182
    • Heim, R.1    Tsien, R.Y.2
  • 16
    • 0031914895 scopus 로고    scopus 로고
    • Steric hindrance mutagenesis versus alanine scan in mapping of ligand binding sites in the tachykinin NK1 receptor
    • Holst B., Zoffmann S., Elling C. E., Hjorth S. A. and Schwartz T. W. (1998) Steric hindrance mutagenesis versus alanine scan in mapping of ligand binding sites in the tachykinin NK1 receptor. Mol. Pharmacol. 53, 166-175.
    • (1998) Mol. Pharmacol , vol.53 , pp. 166-175
    • Holst, B.1    Zoffmann, S.2    Elling, C.E.3    Hjorth, S.A.4    Schwartz, T.W.5
  • 17
    • 0029165752 scopus 로고
    • Identification of residues involved in ligand binding to the neurokinin-2 receptor
    • Huang R. R., Vicario P. P., Strader C. D. and Fong T. M. (1995) Identification of residues involved in ligand binding to the neurokinin-2 receptor. Biochemistry 34, 10 048-10 055.
    • (1995) Biochemistry , vol.34
    • Huang, R.R.1    Vicario, P.P.2    Strader, C.D.3    Fong, T.M.4
  • 18
    • 0038334965 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer to probe human M1 muscarinic receptor structure and drug binding properties
    • Ilien B., Franchet C., Bernard P., Morisset S., Weill C. O., Bourguignon J. J., Hibert M. and Galzi J. L. (2003) Fluorescence resonance energy transfer to probe human M1 muscarinic receptor structure and drug binding properties. J. Neurochem. 85, 768-778.
    • (2003) J. Neurochem , vol.85 , pp. 768-778
    • Ilien, B.1    Franchet, C.2    Bernard, P.3    Morisset, S.4    Weill, C.O.5    Bourguignon, J.J.6    Hibert, M.7    Galzi, J.L.8
  • 19
    • 0034193130 scopus 로고    scopus 로고
    • Using green fluorescent proteins to study G-protein-coupled receptor localization and trafficking
    • Kallal L. and Benovic J. L. (2000) Using green fluorescent proteins to study G-protein-coupled receptor localization and trafficking. Trends Pharmacol. Sci. 21, 175-180.
    • (2000) Trends Pharmacol. Sci , vol.21 , pp. 175-180
    • Kallal, L.1    Benovic, J.L.2
  • 20
    • 0032773556 scopus 로고    scopus 로고
    • Structure-activity studies on cysteine-substituted neurokinin A analogs
    • Labrou N. E., Mello L. V., Rigden D. J., Keen J. N. and Findlay J. B. (1999) Structure-activity studies on cysteine-substituted neurokinin A analogs. Peptides 20, 795-801.
    • (1999) Peptides , vol.20 , pp. 795-801
    • Labrou, N.E.1    Mello, L.V.2    Rigden, D.J.3    Keen, J.N.4    Findlay, J.B.5
  • 21
    • 0035851203 scopus 로고    scopus 로고
    • Interaction of Met297 in the seventh transmembrane segment of the tachykinin NK2 receptor with neurokinin A
    • Labrou N. E., Bhogal N., Hurrell C. R. and Findlay J. B. (2001) Interaction of Met297 in the seventh transmembrane segment of the tachykinin NK2 receptor with neurokinin A. J. Biol. Chem. 276, 37 944-37 949.
    • (2001) J. Biol. Chem , vol.276
    • Labrou, N.E.1    Bhogal, N.2    Hurrell, C.R.3    Findlay, J.B.4
  • 22
    • 0025763316 scopus 로고
    • Fluorescence energy transfer distance measurements using site-directed single cysteine mutants. The membrane insertion of colicin A
    • Lakey J. H., Baty D. and Pattus F. (1991) Fluorescence energy transfer distance measurements using site-directed single cysteine mutants. The membrane insertion of colicin A.. J. Mol. Biol. 218, 639-653.
    • (1991) J. Mol. Biol , vol.218 , pp. 639-653
    • Lakey, J.H.1    Baty, D.2    Pattus, F.3
  • 23
    • 0036830604 scopus 로고    scopus 로고
    • Mutations in the extracellular amino-terminal domain of the NK2 neurokinin receptor abolish cAMP signaling but preserve intracellular calcium responses
    • Lecat S., Bucher B., Mely Y. and Galzi J. L. (2002) Mutations in the extracellular amino-terminal domain of the NK2 neurokinin receptor abolish cAMP signaling but preserve intracellular calcium responses. J. Biol. Chem. 277, 42 034-42 048.
    • (2002) J. Biol. Chem , vol.277
    • Lecat, S.1    Bucher, B.2    Mely, Y.3    Galzi, J.L.4
  • 24
    • 0028861701 scopus 로고
    • Mapping peptide-binding domains of the substance P (NK-1) receptor from P388D1 cells with photolabile agonists
    • Li Y. M., Marnerakis M., Stimson E. R. and Maggio J. E. (1995) Mapping peptide-binding domains of the substance P (NK-1) receptor from P388D1 cells with photolabile agonists. J. Biol. Chem. 270, 1213-1220.
    • (1995) J. Biol. Chem , vol.270 , pp. 1213-1220
    • Li, Y.M.1    Marnerakis, M.2    Stimson, E.R.3    Maggio, J.E.4
  • 25
    • 0034840435 scopus 로고    scopus 로고
    • A novel tachykinin NK2 receptor antagonist prevents motility-stimulating effects of neurokinin A in small intestine
    • Lordal M., Navalesi G., Theodorsson E., Maggi C. A. and Hellstrom P. M. (2001) A novel tachykinin NK2 receptor antagonist prevents motility-stimulating effects of neurokinin A in small intestine. Br. J. Pharmacol. 134, 215-223.
    • (2001) Br. J. Pharmacol , vol.134 , pp. 215-223
    • Lordal, M.1    Navalesi, G.2    Theodorsson, E.3    Maggi, C.A.4    Hellstrom, P.M.5
  • 26
    • 0030061488 scopus 로고    scopus 로고
    • The role of spinal neurokinin-2 receptors in the processing of nociceptive information from the joint and in the generation and maintenance of inflammation-evoked hyperexcitability of dorsal horn neurons in the rat
    • Neugebauer V., Rumenapp P. and Schaible H. G. (1996) The role of spinal neurokinin-2 receptors in the processing of nociceptive information from the joint and in the generation and maintenance of inflammation-evoked hyperexcitability of dorsal horn neurons in the rat. Eur. J. Neurosci. 8, 249-260.
    • (1996) Eur. J. Neurosci , vol.8 , pp. 249-260
    • Neugebauer, V.1    Rumenapp, P.2    Schaible, H.G.3
  • 27
    • 0034604451 scopus 로고    scopus 로고
    • Crystal structure of rhodopsin: A G protein-coupled receptor [see comments]
    • Palczewski K., Kumasaka T., Hori T. et al. (2000) Crystal structure of rhodopsin: A G protein-coupled receptor [see comments]. Science 289, 739-745.
    • (2000) Science , vol.289 , pp. 739-745
    • Palczewski, K.1    Kumasaka, T.2    Hori, T.3
  • 29
    • 0028589913 scopus 로고
    • Receptors and antagonists for substance P and related peptides
    • Regoli D., Boudon A. and Fauchere J. L. (1994) Receptors and antagonists for substance P and related peptides. Pharmacol. Rev. 46, 551-599.
    • (1994) Pharmacol. Rev , vol.46 , pp. 551-599
    • Regoli, D.1    Boudon, A.2    Fauchere, J.L.3
  • 31
    • 0037450507 scopus 로고    scopus 로고
    • Autoradiographic distribution of tachykinin NK2 binding sites in the rat brain: Comparison with NK1 and NK3 binding sites
    • Saffroy M., Torrens Y., Glowinski J. and Beaujouan J. C. (2003) Autoradiographic distribution of tachykinin NK2 binding sites in the rat brain: comparison with NK1 and NK3 binding sites. Neuroscience 116, 761-773.
    • (2003) Neuroscience , vol.116 , pp. 761-773
    • Saffroy, M.1    Torrens, Y.2    Glowinski, J.3    Beaujouan, J.C.4
  • 32
    • 0024786847 scopus 로고
    • Molecular characterization of rat substance K receptor and its mRNAs
    • Sasai Y. and Nakanishi S. (1989) Molecular characterization of rat substance K receptor and its mRNAs. Biochem. Biophys. Res. Commun. 165, 695-702.
    • (1989) Biochem. Biophys. Res. Commun , vol.165 , pp. 695-702
    • Sasai, Y.1    Nakanishi, S.2
  • 33
    • 0024322308 scopus 로고
    • Expression of substance P/neurokinin A-encoding preprotachykinin messenger ribonucleic acids in the rat enteric nervous system
    • Sternini C., Anderson K., Frantz G., Krause J. E. and Brecha N. (1989) Expression of substance P/neurokinin A-encoding preprotachykinin messenger ribonucleic acids in the rat enteric nervous system. Gastroenterology 97, 348-356.
    • (1989) Gastroenterology , vol.97 , pp. 348-356
    • Sternini, C.1    Anderson, K.2    Frantz, G.3    Krause, J.E.4    Brecha, N.5
  • 34
    • 0028942967 scopus 로고
    • Probing the binding domain of the NK2 receptor with fluorescent ligands: Evidence that heptapeptide agonists and antagonists bind differently
    • Turcatti G., Vogel H. and Chollet A. (1995) Probing the binding domain of the NK2 receptor with fluorescent ligands: evidence that heptapeptide agonists and antagonists bind differently. Biochemistry 34, 3972-3980.
    • (1995) Biochemistry , vol.34 , pp. 3972-3980
    • Turcatti, G.1    Vogel, H.2    Chollet, A.3
  • 35
    • 0029838186 scopus 로고    scopus 로고
    • Probing the structure and function of the tachykinin neurokinin-2 receptor through biosynthetic incorporation of fluorescent amino acids at specific sites
    • Turcatti G., Nemeth K., Edgerton M. D., Meseth U., Talabot F., Peitsch M., Knowles J., Vogel H. and Chollet A. (1996) Probing the structure and function of the tachykinin neurokinin-2 receptor through biosynthetic incorporation of fluorescent amino acids at specific sites. J. Biol. Chem. 271, 19 991-19 998.
    • (1996) J. Biol. Chem , vol.271
    • Turcatti, G.1    Nemeth, K.2    Edgerton, M.D.3    Meseth, U.4    Talabot, F.5    Peitsch, M.6    Knowles, J.7    Vogel, H.8    Chollet, A.9
  • 36
    • 0030826420 scopus 로고    scopus 로고
    • Turcatti G., Zoffmann S., Lowe J. A.III., Drozda S. E., Chassaing G., Schwartz T. W. and Chollet A. (1997) Characterization of nonpeptide antagonist and peptide agonist binding sites of the NK1 receptor with fluorescent ligands. J. Biol. Chem. 272, 21 167-21 175.
    • Turcatti G., Zoffmann S., Lowe J. A.III., Drozda S. E., Chassaing G., Schwartz T. W. and Chollet A. (1997) Characterization of nonpeptide antagonist and peptide agonist binding sites of the NK1 receptor with fluorescent ligands. J. Biol. Chem. 272, 21 167-21 175.
  • 38
    • 0031815845 scopus 로고    scopus 로고
    • The effect of the NK2 tachykinin receptor antagonist SR 48968 (saredutant) on neurokinin A-induced bronchoconstriction in asthmatics
    • Van Schoor J., Joos G. F., Chasson B. L., Brouard R. J. and Pauwels R. A. (1998) The effect of the NK2 tachykinin receptor antagonist SR 48968 (saredutant) on neurokinin A-induced bronchoconstriction in asthmatics. Eur. Respir. J. 12, 17-23.
    • (1998) Eur. Respir. J , vol.12 , pp. 17-23
    • Van Schoor, J.1    Joos, G.F.2    Chasson, B.L.3    Brouard, R.J.4    Pauwels, R.A.5
  • 39
    • 0033621359 scopus 로고    scopus 로고
    • Subcellular compartmentalization of activation and desensitization of responses mediated by NK2 neurokinin receptors
    • Vollmer J. Y., Alix P., Chollet A., Takeda K. and Galzi J. L. (1999) Subcellular compartmentalization of activation and desensitization of responses mediated by NK2 neurokinin receptors. J. Biol. Chem. 274, 37 915-37 922.
    • (1999) J. Biol. Chem , vol.274
    • Vollmer, J.Y.1    Alix, P.2    Chollet, A.3    Takeda, K.4    Galzi, J.L.5
  • 40
    • 0032560139 scopus 로고    scopus 로고
    • Membrane-induced secondary structures of neuropeptides: A comparison of the solution conformations adopted by agonists and antagonists of the mammalian tachykinin NK1 receptor
    • Whitehead T. L., McNair S. D., Hadden C. E., Young J. K. and Hicks R. P. (1998) Membrane-induced secondary structures of neuropeptides: a comparison of the solution conformations adopted by agonists and antagonists of the mammalian tachykinin NK1 receptor. J. Med. Chem. 41, 1497-1506.
    • (1998) J. Med. Chem , vol.41 , pp. 1497-1506
    • Whitehead, T.L.1    McNair, S.D.2    Hadden, C.E.3    Young, J.K.4    Hicks, R.P.5
  • 41
    • 0034332431 scopus 로고    scopus 로고
    • Hemokinin is a hematopoietic-specific tachykinin that regulates B lymphopoiesis
    • Zhang Y., Lu L., Furlonger C., Wu G. E. and Paige C. J. (2000) Hemokinin is a hematopoietic-specific tachykinin that regulates B lymphopoiesis. Nat. Immunol. 1, 392-397.
    • (2000) Nat. Immunol , vol.1 , pp. 392-397
    • Zhang, Y.1    Lu, L.2    Furlonger, C.3    Wu, G.E.4    Paige, C.J.5


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