ACS Publications. Most Trusted. Most Cited. Most Read
My Activity
CONTENT TYPES

Figure 1Loading Img

Identification of Residues Involved in Ligand Binding to the Neurokinin-2 Receptor

Cite this: Biochemistry 1995, 34, 31, 10048–10055
Publication Date (Print):August 8, 1995
https://doi.org/10.1021/bi00031a029
    ACS Legacy Archive

    Article Views

    79

    Altmetric

    -

    Citations

    LEARN ABOUT THESE METRICS
    Other access options

    Note: In lieu of an abstract, this is the article's first page.

    Free first page

    Read this article

    To access this article, please review the available access options below.

    Get instant access

    Purchase Access

    Read this article for 48 hours. Check out below using your ACS ID or as a guest.

    Recommended

    Access through Your Institution

    You may have access to this article through your institution.

    Your institution does not have access to this content. You can change your affiliated institution below.

    Cited By

    This article is cited by 60 publications.

    1. Anjali D. Ganjiwale, Gita Subba Rao, and Sudha M. Cowsik . Molecular Modeling of Neurokinin B and Tachykinin NK3 Receptor Complex. Journal of Chemical Information and Modeling 2011, 51 (11) , 2932-2938. https://doi.org/10.1021/ci2000264
    2. Indu R. Chandrashekaran, Gita Subba Rao and Sudha M. Cowsik . Molecular Modeling of the Peptide Agonist-Binding Site in a Neurokinin-2 Receptor. Journal of Chemical Information and Modeling 2009, 49 (7) , 1734-1740. https://doi.org/10.1021/ci900055x
    3. David E. Nichols and Charles D. Nichols . Serotonin Receptors. Chemical Reviews 2008, 108 (5) , 1614-1641. https://doi.org/10.1021/cr078224o
    4. Nirmala Bhogal,, Frank E. Blaney,, Paul M. Ingley,, James Rees, and, John B. C. Findlay. Evidence for the Proximity of the Extreme N-Terminus of the Neurokinin-2 (NK2) Tachykinin Receptor to Cys167 in the Putative Fourth Transmembrane Helix. Biochemistry 2004, 43 (11) , 3027-3038. https://doi.org/10.1021/bi035475s
    5. Mark K. Dean,, Christopher Higgs,, Richard E. Smith,, Robert P. Bywater,, Christopher R. Snell,, Paul D. Scott,, Graham J. G. Upton,, Trevor J. Howe, and, Christopher A. Reynolds. Dimerization of G-Protein-Coupled Receptors. Journal of Medicinal Chemistry 2001, 44 (26) , 4595-4614. https://doi.org/10.1021/jm010290+
    6. Josephine Liu,, Dennis J. Underwood,, Margaret A. Cascieri,, Susan P. Rohrer,, Louis-David Cantin,, Gary Chicchi,, Amos B. Smith, III, and, Ralph Hirschmann. Synthesis of a Substance P Antagonist with a Somatostatin Scaffold:  Factors Affecting Agonism/Antagonism at GPCRs and the Role of Pseudosymmetry. Journal of Medicinal Chemistry 2000, 43 (21) , 3827-3831. https://doi.org/10.1021/jm000316h
    7. Dmitry S. Gembitsky,, Mark Murnin,, Ferenc L. Ötvös,, James Allen,, Richard F. Murphy, and, Sándor Lovas. Importance of the Aromatic Residue at Position 6 of [Nle10]Neurokinin A(4−10) for Binding to the NK-2 Receptor and Receptor Activation. Journal of Medicinal Chemistry 1999, 42 (15) , 3004-3007. https://doi.org/10.1021/jm9807151
    8. Giuliano Alagona and, Caterina Ghio, , Susanna Monti. Ab Initio Investigation of the Methylimidazole−Indole Complexes as Models of the Histidine−Tryptophan Pair. The Journal of Physical Chemistry A 1998, 102 (30) , 6152-6160. https://doi.org/10.1021/jp980327a
    9. Tracy L. Whitehead,, Sharon D. McNair,, Chad E. Hadden,, John K. Young, and, Rickey P. Hicks. Membrane-Induced Secondary Structures of Neuropeptides:  A Comparison of the Solution Conformations Adopted by Agonists and Antagonists of the Mammalian Tachykinin NK1 Receptor. Journal of Medicinal Chemistry 1998, 41 (9) , 1497-1506. https://doi.org/10.1021/jm970789x
    10. Anjali Ganjiwale, Sudha M. Cowsik. Membrane‐induced structure of novel human tachykinin hemokinin‐1 (h HK 1). Biopolymers 2015, 103 (12) , 702-710. https://doi.org/10.1002/bip.22734
    11. Pari Malherbe, Frédéric Knoflach, Anne Marcuz, Claudia Bohnert, Michael Weber, Henner Knust, Hasane Ratni, Will Spooren, Theresa M. Ballard, Caterina Bissantz. Mapping the binding pocket of a novel, high-affinity, slow dissociating tachykinin NK3 receptor antagonist: Biochemical and electrophysiological characterization. Neuropharmacology 2014, 86 , 259-272. https://doi.org/10.1016/j.neuropharm.2014.07.017
    12. Pari Malherbe, Olivier Roche, Anne Marcuz, Claudia Kratzeisen, Joseph G. Wettstein, Caterina Bissantz. Mapping the Binding Pocket of Dual Antagonist Almorexant to Human Orexin 1 and Orexin 2 Receptors: Comparison with the Selective OX 1 Antagonist SB-674042 and the Selective OX 2 Antagonist N -Ethyl-2-[(6-methoxy-pyridin-3-yl)-(toluene-2-sulfonyl)-amino]- N -pyridin-3-ylmethyl-acetamide (EMPA). Molecular Pharmacology 2010, 78 (1) , 81-93. https://doi.org/10.1124/mol.110.064584
    13. Liping Yan, Brian J. Holleran, Pierre Lavigne, Emanuel Escher, Gaétan Guillemette, Richard Leduc. Analysis of Transmembrane Domains 1 and 4 of the Human Angiotensin II AT1 Receptor by Cysteine-scanning Mutagenesis. Journal of Biological Chemistry 2010, 285 (4) , 2284-2293. https://doi.org/10.1074/jbc.M109.077180
    14. Stefania Meini, Francesca Bellucci, Claudio Catalani, Paola Cucchi, Alessandro Giolitti, Paolo Santicioli, Sandro Giuliani. Multifaceted Approach to Determine the Antagonist Molecular Mechanism and Interaction of Ibodutant ([1-(2-Phenyl-1 R -{[1-(tetrahydropyran-4-ylmethyl)-piperidin-4-ylmethyl]-carbamoyl}-ethylcarbamoyl)-cyclopentyl]-amide) at the Human Tachykinin NK 2 Receptor. Journal of Pharmacology and Experimental Therapeutics 2009, 329 (2) , 486-495. https://doi.org/10.1124/jpet.108.150201
    15. Ingela Ahlstedt, Susanna Engberg, John Smith, Chris Perrey, Adrian Moody, John Morten, Maria Lagerström-Fermér, Tomas Drmota, Bengt von Mentzer, Ingrid Påhlman, Erik Lindström. Occurrence and pharmacological characterization of four human tachykinin NK2 receptor variants. Biochemical Pharmacology 2008, 76 (4) , 476-481. https://doi.org/10.1016/j.bcp.2008.06.003
    16. Pari Malherbe, Caterina Bissantz, Anne Marcuz, Claudia Kratzeisen, Marie-Thérèse Zenner, Joseph G. Wettstein, Hasane Ratni, Claus Riemer, Will Spooren. Me-Talnetant and Osanetant Interact within Overlapping but Not Identical Binding Pockets in the Human Tachykinin Neurokinin 3 Receptor Transmembrane Domains. Molecular Pharmacology 2008, 73 (6) , 1736-1750. https://doi.org/10.1124/mol.107.042754
    17. Sannah Zoffmann, Sonia Bertrand, Quoc‐Tuan Do, Daniel Bertrand, Didier Rognan, Marcel Hibert, Jean‐Luc Galzi. Topological analysis of the complex formed between neurokinin A and the NK2 tachykinin receptor. Journal of Neurochemistry 2007, 101 (2) , 506-516. https://doi.org/10.1111/j.1471-4159.2007.04473.x
    18. Michael R. Braden, Jason C. Parrish, John C. Naylor, David E. Nichols. Molecular Interaction of Serotonin 5-HT 2A Receptor Residues Phe339 (6.51) and Phe340 (6.52) with Superpotent N -Benzyl Phenethylamine Agonists. Molecular Pharmacology 2006, 70 (6) , 1956-1964. https://doi.org/10.1124/mol.106.028720
    19. Jiaping Zhang, Chun-Pyn Shen, Jing C. Xiao, Thomas J. Lanza, Linus S. Lin, Barbara E. Francis, Tung M. Fong, Richard Z. Chen. Effects of mutations at conserved TM II residues on ligand binding and activation of mouse 5-HT6 receptor. European Journal of Pharmacology 2006, 534 (1-3) , 77-82. https://doi.org/10.1016/j.ejphar.2006.01.049
    20. Shaomin Tian, Won-Tak Choi, Dongxiang Liu, James Pesavento, Youli Wang, Jing An, Joseph G. Sodroski, Ziwei Huang. Distinct Functional Sites for Human Immunodeficiency Virus Type 1 and Stromal Cell-Derived Factor 1α on CXCR4 Transmembrane Helical Domains. Journal of Virology 2005, 79 (20) , 12667-12673. https://doi.org/10.1128/JVI.79.20.12667-12673.2005
    21. Stefania Meini, Claudio Catalani, Francesca Bellucci, Paola Cucchi, Sandro Giuliani, Sabrina Zappitelli, Luigi Rotondaro, Franco Pasqui, Antonio Guidi, Maria Altamura, Alessandro Giolitti, Carlo Alberto Maggi. Pharmacology of an original and selective nonpeptide antagonist ligand for the human tachykinin NK2 receptor. European Journal of Pharmacology 2005, 516 (2) , 104-111. https://doi.org/10.1016/j.ejphar.2005.04.033
    22. Shih-Chung Huang, Bradley Undem, Vijaya Korlipara. Design and synthesis of substituted N-methylbenzamide analogues derived from SR 48,968 as neurokinin-2 receptor antagonists. Bioorganic & Medicinal Chemistry Letters 2004, 14 (18) , 4779-4782. https://doi.org/10.1016/j.bmcl.2004.06.053
    23. Stefania Meini, Francesca Bellucci, Claudio Catalani, Paola Cucchi, Riccardo Patacchini, Luigi Rotondaro, Maria Altamura, Sandro Giuliani, Alessandro Giolitti, Carlo Alberto Maggi. Mutagenesis at the human tachykinin NK2 receptor to define the binding site of a novel class of antagonists. European Journal of Pharmacology 2004, 488 (1-3) , 61-69. https://doi.org/10.1016/j.ejphar.2004.02.016
    24. Indu R. Chandrashekar, Sudha M. Cowsik. Three-Dimensional Structure of the Mammalian Tachykinin Peptide Neurokinin A Bound to Lipid Micelles. Biophysical Journal 2003, 85 (6) , 4002-4011. https://doi.org/10.1016/S0006-3495(03)74814-0
    25. Daniel Pisera, Marianela Candolfi, Andrea De Laurentiis, Adriana Seilicovich. Characterization of tachykinin NK2 receptor in the anterior pituitary gland. Life Sciences 2003, 73 (19) , 2421-2432. https://doi.org/10.1016/S0024-3205(03)00650-7
    26. Fiona J Warner, Robert C Miller, Elizabeth Burcher. Human tachykinin NK 2 receptor: A comparative study of the colon and urinary bladder. Clinical and Experimental Pharmacology and Physiology 2003, 30 (9) , 632-639. https://doi.org/10.1046/j.1440-1681.2003.03887.x
    27. Sandra Lecat, Bernard Bucher, Yves Mely, Jean-Luc Galzi. Mutations in the Extracellular Amino-terminal Domain of the NK2 Neurokinin Receptor Abolish cAMP Signaling but Preserve Intracellular Calcium Responses. Journal of Biological Chemistry 2002, 277 (44) , 42034-42048. https://doi.org/10.1074/jbc.M203606200
    28. W.B. Church, K.A. Jones, D.A. Kuiper, J. Shine, T.P. Iismaa. Molecular modelling and site-directed mutagenesis of human GALR1 galanin receptor defines determinants of receptor subtype specificity. Protein Engineering, Design and Selection 2002, 15 (4) , 313-323. https://doi.org/10.1093/protein/15.4.313
    29. Jacky Marie, Eric Richard, Didier Pruneau, Jean-Luc Paquet, Christian Siatka, Renée Larguier, Cecilia Poncé, Philippe Vassault, Thierry Groblewski, Bernard Maigret, Jean-Claude Bonnafous. Control of Conformational Equilibria in the Human B2 Bradykinin Receptor. Journal of Biological Chemistry 2001, 276 (44) , 41100-41111. https://doi.org/10.1074/jbc.M104875200
    30. Nick E. Labrou, Nirmala Bhogal, Craig R. Hurrell, John B.C. Findlay. Interaction of Met297 in the Seventh Transmembrane Segment of the Tachykinin NK2 Receptor with Neurokinin A. Journal of Biological Chemistry 2001, 276 (41) , 37944-37949. https://doi.org/10.1074/jbc.M106330200
    31. Tania Palanche, Brigitte Ilien, Sannah Zoffmann, Marie-Pierre Reck, Bernard Bucher, Stuart J. Edelstein, Jean-Luc Galzi. The Neurokinin A Receptor Activates Calcium and cAMP Responses through Distinct Conformational States. Journal of Biological Chemistry 2001, 276 (37) , 34853-34861. https://doi.org/10.1074/jbc.M104363200
    32. Mohammed A. Ali, Nirmala Bhogal, Colin W.G. Fishwick, John B.C. Findlay. Spatial requirements of the antagonist binding site of the NK2 receptor. Bioorganic & Medicinal Chemistry Letters 2001, 11 (6) , 819-822. https://doi.org/10.1016/S0960-894X(01)00074-9
    33. S.R. Vigna. The N-terminal domain of substance P is required for complete homologous desensitization but not phosphorylation of the rat neurokinin-1 receptor. Neuropeptides 2001, 35 (1) , 24-31. https://doi.org/10.1054/npep.2000.0840
    34. Alessandro Giolitti, Paola Cucchi, Anna Rita Renzetti, Luigi Rotondaro, Sabrina Zappitelli, Carlo Alberto Maggi. Molecular determinants of peptide and nonpeptide NK-2 receptor antagonists binding sites of the human tachykinin NK-2 receptor by site-directed mutagenesis. Neuropharmacology 2000, 39 (8) , 1422-1429. https://doi.org/10.1016/S0028-3908(00)00008-3
    35. Nathalie Cotte, Marie‐Noëlle Balestre, André Aumelas, Eve Mahé, Sylvie Phalipou, Denis Morin, Marcel Hibert, Maurice Manning, Thierry Durroux, Claude Barberis, Bernard Mouillac. Conserved aromatic residues in the transmembrane region VI of the V 1a vasopressin receptor differentiate agonist vs. antagonist ligand binding. European Journal of Biochemistry 2000, 267 (13) , 4253-4263. https://doi.org/10.1046/j.1432-1033.2000.01472.x
    36. Ulrik Gether. Uncovering Molecular Mechanisms Involved in Activation of G Protein-Coupled Receptors. Endocrine Reviews 2000, 21 (1) , 90-113. https://doi.org/10.1210/edrv.21.1.0390
    37. D. M. Perez, S. S. Karnik. Mechanisms of Receptor Activation and the Relationship to Receptor Structure. 2000, 283-309. https://doi.org/10.1007/978-3-642-57081-0_11
    38. Scott Greenfeder, Boonlert Cheewatrakoolpong, Motasim Billah, Robert W Egan, Elizabeth Keene, Nicholas J Murgolo, John C Anthes. The neurokinin-1 and neurokinin-2 receptor binding sites of MDL103,392 differ. Bioorganic & Medicinal Chemistry 1999, 7 (12) , 2867-2876. https://doi.org/10.1016/S0968-0896(99)00220-5
    39. Jean-Yves Vollmer, Philippe Alix, André Chollet, Kenneth Takeda, Jean-Luc Galzi. Subcellular Compartmentalization of Activation and Desensitization of Responses Mediated by NK2 Neurokinin Receptors. Journal of Biological Chemistry 1999, 274 (53) , 37915-37922. https://doi.org/10.1074/jbc.274.53.37915
    40. Paul Gouldson, Pascale Legoux, Christine Carillon, Bruno Delpech, Gérard Le Fur, Pascual Ferrara, David Shire. Contrasting roles of Leu356 in the human CCK1 receptor for antagonist SR 27897 and agonist SR 146131 binding. European Journal of Pharmacology 1999, 383 (3) , 339-346. https://doi.org/10.1016/S0014-2999(99)00612-3
    41. Alfredo Ulloa-Aguirre, Dinesh Stanislaus, Jo Ann Janovick, P.Michael Conn. Structure-Activity Relationships of G Protein-Coupled Receptors. Archives of Medical Research 1999, 30 (6) , 420-435. https://doi.org/10.1016/S0188-0128(99)00041-X
    42. Anna Rita Renzetti, Rose-Marie Catalioto, Cristina Carloni, Marco Criscuoli, Paola Cucchi, Alessandro Giolitti, Sabrina Zappitelli, Luigi Rotondaro, Carlo Alberto Maggi. Effects of tyrosine289phenylalanine mutation on binding and functional properties of the human tachykinin NK2 receptor stably expressed in Chinese hamster ovary cells. Biochemical Pharmacology 1999, 57 (8) , 899-906. https://doi.org/10.1016/S0006-2952(98)00373-6
    43. Alfredo Ulloa‐Aguirre, P. Michael Conn. G Protein‐Coupled Receptors and the G Protein Family. 1998, 87-124. https://doi.org/10.1002/cphy.cp070106
    44. David A. Keire, Mitsuo Kobayashi. The orientation and dynamics of substance P in lipid environments. Protein Science 1998, 7 (11) , 2438-2450. https://doi.org/10.1002/pro.5560071122
    45. Sandrine Silvente-Poirot, Chantal Escrieut, Stephen A. Wank. Role of the Extracellular Domains of the Cholecystokinin Receptor in Agonist Binding. Molecular Pharmacology 1998, 54 (2) , 364-371. https://doi.org/10.1124/mol.54.2.364
    46. A.R. Renzetti, R-M. Catalioto, M. Criscuoli, P. Cucchi, A. Lippi, M. Guelfi, L. Quartara, C.A. Maggi. Characterization of [3H]MEN 11420, a Novel Glycosylated Peptide Antagonist Radioligand of the Tachykinin NK2Receptor. Biochemical and Biophysical Research Communications 1998, 248 (1) , 78-82. https://doi.org/10.1006/bbrc.1998.8883
    47. Franca Mancuso, Claudia Costa, Antonio Calignano, Loredana Mariniello, Francesco Rossi, Raffaele Porta, Carla Esposito. Transglutaminase-Synthesized γ-(Glutamyl5) Spermidine Derivative of Substance P Is a Selective Tool for Neurokinin-2 Receptors Characterization. Peptides 1998, 19 (4) , 683-690. https://doi.org/10.1016/S0196-9781(98)00014-X
    48. Helgi B. Schiöth, Ann Fredriksson, Cecilia Carlsson, Philip Yook, Ruta Muceniece, Jarl E.S. Wikberg. Evidence indicating that the extracellular loops of the mouse MC5 receptor do not participate in ligand binding. Molecular and Cellular Endocrinology 1998, 139 (1-2) , 109-115. https://doi.org/10.1016/S0303-7207(98)00067-7
    49. John S. Mills, Heini M. Miettinen, David Barnidge, Michael J. Vlases, Susan Wimer-Mackin, Edward A. Dratz, Jan Sunner, Algirdas J. Jesaitis. Identification of a Ligand Binding Site in the Human Neutrophil Formyl Peptide Receptor Using a Site-specific Fluorescent Photoaffinity Label and Mass Spectrometry. Journal of Biological Chemistry 1998, 273 (17) , 10428-10435. https://doi.org/10.1074/jbc.273.17.10428
    50. Kenneth C. Appell, Thomas D.Y. Chung, Kelli J. Solly, Daniel Chelsky. Biological Characterization of Neurokinin Antagonists Discovered Through Screening of a Combinatorial Library. SLAS Discovery 1998, 3 (1) , 19-27. https://doi.org/10.1177/108705719800300103
    51. Birgitte Holst, Sannah Zoffmann, Christian E. Elling, Siv A. Hjorth, Thue W. Schwartz. Steric Hindrance Mutagenesis versus Alanine Scan in Mapping of Ligand Binding Sites in the Tachykinin NK 1 Receptor. Molecular Pharmacology 1998, 53 (1) , 166-175. https://doi.org/10.1124/mol.53.1.166
    52. Walter K. Vogel, David M. Sheehan, Michael I. Schimerlik. Site-Directed Mutagenesis on the m2 Muscarinic Acetylcholine Receptor: The Significance of Tyr403 in the Binding of Agonists and Functional Coupling. Molecular Pharmacology 1997, 52 (6) , 1087-1094. https://doi.org/10.1124/mol.52.6.1087
    53. Ying-kui Yang, Chris Dickinson, Carrie Haskell-Luevano, Ira Gantz. Molecular Basis for the Interaction of [Nle4,d-Phe7]Melanocyte Stimulating Hormone with the Human Melanocortin-1 Receptor (Melanocyte α-MSH Receptor). Journal of Biological Chemistry 1997, 272 (37) , 23000-23010. https://doi.org/10.1074/jbc.272.37.23000
    54. Helgi B Schiöth, Susanna Petersson, Ruta Muceniece, Michael Szardenings, Jarl E.S Wikberg. Deletions of the N‐terminal regions of the human melanocortin receptors. FEBS Letters 1997, 410 (2-3) , 223-228. https://doi.org/10.1016/S0014-5793(97)00593-0
    55. THUE W. SCHWARTZ, SIGNE PERLMAN, METTE M. ROSENKILDE, SIV A. HJORTH. How Receptor Mutagenesis May Confirm or Confuse Receptor Classification. Annals of the New York Academy of Sciences 1997, 812 (1) , 71-84. https://doi.org/10.1111/j.1749-6632.1997.tb48147.x
    56. Signe Perlman, Claudio M. Costa-Neto, Ayumi A. Miyakawa, Hans T. Schambye, Siv A. Hjorth, Antonio C. M. Paiva, Ralph A. Rivero, William J. Greenlee, Thue W. Schwartz. Dual Agonistic and Antagonistic Property of Nonpeptide Angiotensin AT 1 Ligands: Susceptibility to Receptor Mutations. Molecular Pharmacology 1997, 51 (2) , 301-311. https://doi.org/10.1124/mol.51.2.301
    57. Hanne Hastrup, Thue W. Schwartz. Septide and neurokinin A are high‐affinity ligands on the NK‐1 receptor: evidence from homologous versus heterologous binding analysis. FEBS Letters 1996, 399 (3) , 264-266. https://doi.org/10.1016/S0014-5793(96)01337-3
    58. Ye Tian, Lan-Hsin Wu, Dale L. Oxender, Fu-Zon Chung. The Unpredicted High Affinities of a Large Number of Naturally Occurring Tachykinins for Chimeric NK1/NK3 Receptors Suggest a Role for an Inhibitory Domain in Determining Receptor Specificity. Journal of Biological Chemistry 1996, 271 (34) , 20250-20257. https://doi.org/10.1074/jbc.271.34.20250
    59. Thue W. Schwartz, Mette M. Rosenkilde. Is there a ‘lock’ for all agonist ‘keys’ in 7TM receptors?. Trends in Pharmacological Sciences 1996, 17 (6) , 213-216. https://doi.org/10.1016/0165-6147(96)10017-1
    60. Tung Ming Fong. Mechanistic hypotheses for the activation of G-protein-coupled receptors. Cellular Signalling 1996, 8 (3) , 217-224. https://doi.org/10.1016/0898-6568(95)02057-8

    Pair your accounts.

    Export articles to Mendeley

    Get article recommendations from ACS based on references in your Mendeley library.

    Pair your accounts.

    Export articles to Mendeley

    Get article recommendations from ACS based on references in your Mendeley library.

    You’ve supercharged your research process with ACS and Mendeley!

    STEP 1:
    Click to create an ACS ID

    Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

    Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

    Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

    MENDELEY PAIRING EXPIRED
    Your Mendeley pairing has expired. Please reconnect