Cooperative binding of distamycin-A to DNA in the 2:1 mode
The preference of distamycin-a for A-T rich binding sites has been recognized for many years. NMR was first used to show unambiguously that the closely related drug netropsin bound in the minor groove of B-form DNA. Both NMR and crystallographic studies of complexes of distamycin-A, netropsin, Hoech...
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| Veröffentlicht in: | Journal of the American Chemical Society 1992-01, Vol.114 (3), p.1080-1081 |
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| container_title | Journal of the American Chemical Society |
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| creator | Fagan, Patricia Wemmer, David E |
| description | The preference of distamycin-a for A-T rich binding sites has been recognized for many years. NMR was first used to show unambiguously that the closely related drug netropsin bound in the minor groove of B-form DNA. Both NMR and crystallographic studies of complexes of distamycin-A, netropsin, Hoechst 33258, and SN-6999 have been carried out. In all of these studies to date, the drugs are bound deep in the minor groove of an A-T segment. Where the drug is bound, the structure of the minor groove closely matches the shape and width of the drug molecule. In several of the DNAs studied crystallographically, the groove is found to be equally narrow without the drug present. |
| doi_str_mv | 10.1021/ja00029a042 |
| format | Article |
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NMR was first used to show unambiguously that the closely related drug netropsin bound in the minor groove of B-form DNA. Both NMR and crystallographic studies of complexes of distamycin-A, netropsin, Hoechst 33258, and SN-6999 have been carried out. In all of these studies to date, the drugs are bound deep in the minor groove of an A-T segment. Where the drug is bound, the structure of the minor groove closely matches the shape and width of the drug molecule. In several of the DNAs studied crystallographically, the groove is found to be equally narrow without the drug present.</description><identifier>ISSN: 0002-7863</identifier><identifier>EISSN: 1520-5126</identifier><identifier>DOI: 10.1021/ja00029a042</identifier><identifier>CODEN: JACSAT</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Antibiotics. Antiinfectious agents. 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Am. Chem. Soc</addtitle><description>The preference of distamycin-a for A-T rich binding sites has been recognized for many years. NMR was first used to show unambiguously that the closely related drug netropsin bound in the minor groove of B-form DNA. Both NMR and crystallographic studies of complexes of distamycin-A, netropsin, Hoechst 33258, and SN-6999 have been carried out. In all of these studies to date, the drugs are bound deep in the minor groove of an A-T segment. Where the drug is bound, the structure of the minor groove closely matches the shape and width of the drug molecule. In several of the DNAs studied crystallographically, the groove is found to be equally narrow without the drug present.</description><subject>Antibiotics. Antiinfectious agents. Antiparasitic agents</subject><subject>Antiviral agents</subject><subject>Biological and medical sciences</subject><subject>Medical sciences</subject><subject>Pharmacology. 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Antiinfectious agents. Antiparasitic agents</topic><topic>Antiviral agents</topic><topic>Biological and medical sciences</topic><topic>Medical sciences</topic><topic>Pharmacology. Drug treatments</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fagan, Patricia</creatorcontrib><creatorcontrib>Wemmer, David E</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><jtitle>Journal of the American Chemical Society</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fagan, Patricia</au><au>Wemmer, David E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cooperative binding of distamycin-A to DNA in the 2:1 mode</atitle><jtitle>Journal of the American Chemical Society</jtitle><addtitle>J. Am. Chem. Soc</addtitle><date>1992-01-01</date><risdate>1992</risdate><volume>114</volume><issue>3</issue><spage>1080</spage><epage>1081</epage><pages>1080-1081</pages><issn>0002-7863</issn><eissn>1520-5126</eissn><coden>JACSAT</coden><abstract>The preference of distamycin-a for A-T rich binding sites has been recognized for many years. NMR was first used to show unambiguously that the closely related drug netropsin bound in the minor groove of B-form DNA. Both NMR and crystallographic studies of complexes of distamycin-A, netropsin, Hoechst 33258, and SN-6999 have been carried out. In all of these studies to date, the drugs are bound deep in the minor groove of an A-T segment. Where the drug is bound, the structure of the minor groove closely matches the shape and width of the drug molecule. In several of the DNAs studied crystallographically, the groove is found to be equally narrow without the drug present.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><doi>10.1021/ja00029a042</doi><tpages>2</tpages></addata></record> |
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| language | eng |
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| source | American Chemical Society Journals |
| subjects | Antibiotics. Antiinfectious agents. Antiparasitic agents Antiviral agents Biological and medical sciences Medical sciences Pharmacology. Drug treatments |
| title | Cooperative binding of distamycin-A to DNA in the 2:1 mode |
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