Different binding epitopes on the NK1 receptor for substance P and a non-peptide antagonist
NON-PEPTIDE ligands for peptide receptors have been discovered in several systems through file screening programs 1–6 , but the mechanism of action for these candidate drugs is obscure as they do not chemically resemble the native peptides. The compound CP 96345 is a high-affinity, non-peptide antag...
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| Veröffentlicht in: | Nature (London) 1993-03, Vol.362 (6418), p.345-348 |
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| creator | Gether, Ulrik Johansen, Teit E. Snider, R. Michael Lowe, John A. Nakanishi, Shigetada Schwartz, Thue W. |
| description | NON-PEPTIDE ligands for peptide receptors have been discovered in several systems through file screening programs
1–6
, but the mechanism of action for these candidate drugs is obscure as they do not chemically resemble the native peptides. The compound CP 96345 is a high-affinity, non-peptide antagonist of the substance P (NK
1
) receptor
4,5,7
, which is important in pain perception and neurogenic inflammation
8–11
. Here we identify epitopes on the NK
1
, receptor responsible for the specific binding of CP 96345 by systematic exchange of corresponding segments between the NK
1
, receptor and the homologous NK
3
(neurokinin B) receptor, which does not bind the non-peptide ligand. Non-conserved residues, in two epitopes around the top of transmembrane segment V and in one epitope at the top of transmembrane segment VI, are essential for the specific action of CP 96345 on the NK
1
, receptor, but are surprisingly not important for the binding of the natural peptide ligand, substance P. Susceptibility to the non-peptide antagonists can be conveyed to the previously unresponsive NK
3
receptor by mutational transfer of this discontinuous epitope from the NK
1
, receptor. |
| doi_str_mv | 10.1038/362345a0 |
| format | Article |
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1–6
, but the mechanism of action for these candidate drugs is obscure as they do not chemically resemble the native peptides. The compound CP 96345 is a high-affinity, non-peptide antagonist of the substance P (NK
1
) receptor
4,5,7
, which is important in pain perception and neurogenic inflammation
8–11
. Here we identify epitopes on the NK
1
, receptor responsible for the specific binding of CP 96345 by systematic exchange of corresponding segments between the NK
1
, receptor and the homologous NK
3
(neurokinin B) receptor, which does not bind the non-peptide ligand. Non-conserved residues, in two epitopes around the top of transmembrane segment V and in one epitope at the top of transmembrane segment VI, are essential for the specific action of CP 96345 on the NK
1
, receptor, but are surprisingly not important for the binding of the natural peptide ligand, substance P. Susceptibility to the non-peptide antagonists can be conveyed to the previously unresponsive NK
3
receptor by mutational transfer of this discontinuous epitope from the NK
1
, receptor.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/362345a0</identifier><identifier>PMID: 7681152</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Amino Acid Sequence ; Binding Sites ; Biological and medical sciences ; Biphenyl Compounds - chemistry ; Cell receptors ; Cell structures and functions ; Epitopes ; Fundamental and applied biological sciences. Psychology ; Genetic engineering ; Hormone receptors. Growth factor receptors. Cytokine receptors. Prostaglandin receptors ; Humanities and Social Sciences ; letter ; Molecular and cellular biology ; Molecular Sequence Data ; multidisciplinary ; Proteins ; Receptors, Neurokinin-2 ; Receptors, Neurotransmitter - chemistry ; Recombinant Proteins - chemistry ; Science ; Tachykinins - chemistry</subject><ispartof>Nature (London), 1993-03, Vol.362 (6418), p.345-348</ispartof><rights>Springer Nature Limited 1993</rights><rights>1993 INIST-CNRS</rights><rights>Copyright Macmillan Journals Ltd. Mar 25, 1993</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3490-a9a20e4a2364d2d37b224c3c01adaeafcdb87d779c0ffca14ab07763aad4795f3</citedby><cites>FETCH-LOGICAL-c3490-a9a20e4a2364d2d37b224c3c01adaeafcdb87d779c0ffca14ab07763aad4795f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4654307$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7681152$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gether, Ulrik</creatorcontrib><creatorcontrib>Johansen, Teit E.</creatorcontrib><creatorcontrib>Snider, R. Michael</creatorcontrib><creatorcontrib>Lowe, John A.</creatorcontrib><creatorcontrib>Nakanishi, Shigetada</creatorcontrib><creatorcontrib>Schwartz, Thue W.</creatorcontrib><title>Different binding epitopes on the NK1 receptor for substance P and a non-peptide antagonist</title><title>Nature (London)</title><addtitle>Nature</addtitle><addtitle>Nature</addtitle><description>NON-PEPTIDE ligands for peptide receptors have been discovered in several systems through file screening programs
1–6
, but the mechanism of action for these candidate drugs is obscure as they do not chemically resemble the native peptides. The compound CP 96345 is a high-affinity, non-peptide antagonist of the substance P (NK
1
) receptor
4,5,7
, which is important in pain perception and neurogenic inflammation
8–11
. Here we identify epitopes on the NK
1
, receptor responsible for the specific binding of CP 96345 by systematic exchange of corresponding segments between the NK
1
, receptor and the homologous NK
3
(neurokinin B) receptor, which does not bind the non-peptide ligand. Non-conserved residues, in two epitopes around the top of transmembrane segment V and in one epitope at the top of transmembrane segment VI, are essential for the specific action of CP 96345 on the NK
1
, receptor, but are surprisingly not important for the binding of the natural peptide ligand, substance P. Susceptibility to the non-peptide antagonists can be conveyed to the previously unresponsive NK
3
receptor by mutational transfer of this discontinuous epitope from the NK
1
, receptor.</description><subject>Amino Acid Sequence</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Biphenyl Compounds - chemistry</subject><subject>Cell receptors</subject><subject>Cell structures and functions</subject><subject>Epitopes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genetic engineering</subject><subject>Hormone receptors. Growth factor receptors. Cytokine receptors. Prostaglandin receptors</subject><subject>Humanities and Social Sciences</subject><subject>letter</subject><subject>Molecular and cellular biology</subject><subject>Molecular Sequence Data</subject><subject>multidisciplinary</subject><subject>Proteins</subject><subject>Receptors, Neurokinin-2</subject><subject>Receptors, Neurotransmitter - chemistry</subject><subject>Recombinant Proteins - chemistry</subject><subject>Science</subject><subject>Tachykinins - chemistry</subject><issn>0028-0836</issn><issn>1476-4687</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNplkE9rFEEQxRtR4roKfgGhCSJ6GO1_0z17lJiYkBA9JKcchpru6k2H3e6xe-aQb2-H3USIh6qCej-qHo-Q95x95Ux236QWUrXAXpAFV0Y3SnfmJVkwJrqGdVK_Jm9KuWOMtdyoA3JgdMd5Kxbk5kfwHjPGiQ4huhDXFMcwpRELTZFOt0gvzznNaHGcUqa-VpmHMkG0SH9TiI4CjSk2YwWCw7qZYJ1iKNNb8srDpuC7_VyS65Pjq6PT5uLXz7Oj7xeNlWrFGliBYKhASK2ccNIMQigrLePgAMFbN3TGGbOyzHsLXMHAjNESwCmzar1ckk-7u2NOf2YsU78NxeJmAxHTXHrTaikf2pIcPgPv0pxj9dYLppSWupMV-ryDbE6lZPT9mMMW8n3PWf8Qdv8YdkU_7O_NwxbdE7hPt-of9zoUCxufa2ihPGFKt0oyU7EvO6xUJa4x_7P138u_lTeSnQ</recordid><startdate>19930325</startdate><enddate>19930325</enddate><creator>Gether, Ulrik</creator><creator>Johansen, Teit E.</creator><creator>Snider, R. 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Academic</collection><jtitle>Nature (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gether, Ulrik</au><au>Johansen, Teit E.</au><au>Snider, R. Michael</au><au>Lowe, John A.</au><au>Nakanishi, Shigetada</au><au>Schwartz, Thue W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Different binding epitopes on the NK1 receptor for substance P and a non-peptide antagonist</atitle><jtitle>Nature (London)</jtitle><stitle>Nature</stitle><addtitle>Nature</addtitle><date>1993-03-25</date><risdate>1993</risdate><volume>362</volume><issue>6418</issue><spage>345</spage><epage>348</epage><pages>345-348</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><coden>NATUAS</coden><abstract>NON-PEPTIDE ligands for peptide receptors have been discovered in several systems through file screening programs
1–6
, but the mechanism of action for these candidate drugs is obscure as they do not chemically resemble the native peptides. The compound CP 96345 is a high-affinity, non-peptide antagonist of the substance P (NK
1
) receptor
4,5,7
, which is important in pain perception and neurogenic inflammation
8–11
. Here we identify epitopes on the NK
1
, receptor responsible for the specific binding of CP 96345 by systematic exchange of corresponding segments between the NK
1
, receptor and the homologous NK
3
(neurokinin B) receptor, which does not bind the non-peptide ligand. Non-conserved residues, in two epitopes around the top of transmembrane segment V and in one epitope at the top of transmembrane segment VI, are essential for the specific action of CP 96345 on the NK
1
, receptor, but are surprisingly not important for the binding of the natural peptide ligand, substance P. Susceptibility to the non-peptide antagonists can be conveyed to the previously unresponsive NK
3
receptor by mutational transfer of this discontinuous epitope from the NK
1
, receptor.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>7681152</pmid><doi>10.1038/362345a0</doi><tpages>4</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0028-0836 |
| ispartof | Nature (London), 1993-03, Vol.362 (6418), p.345-348 |
| issn | 0028-0836 1476-4687 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_75633756 |
| source | MEDLINE; Nature; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Binding Sites Biological and medical sciences Biphenyl Compounds - chemistry Cell receptors Cell structures and functions Epitopes Fundamental and applied biological sciences. Psychology Genetic engineering Hormone receptors. Growth factor receptors. Cytokine receptors. Prostaglandin receptors Humanities and Social Sciences letter Molecular and cellular biology Molecular Sequence Data multidisciplinary Proteins Receptors, Neurokinin-2 Receptors, Neurotransmitter - chemistry Recombinant Proteins - chemistry Science Tachykinins - chemistry |
| title | Different binding epitopes on the NK1 receptor for substance P and a non-peptide antagonist |
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