Solution structure of a specific DNA complex of the Myb DNA-binding domain with cooperative recognition helices
The DNA-binding region of Myb consists of three imperfect tandem repeats (R1, R2, and R3). We have determined the solution structure of a specific DNA complex of the minimum DNA-binding domain (R2R3) by heteronuclear multidimensional NMR. Both R2 and R3 contain three helices, and the third helix in...
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| Veröffentlicht in: | Cell 1994-11, Vol.79 (4), p.639-648 |
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| container_title | Cell |
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| creator | Ogata, Kazuhiro Morikawa, Souichi Nakamura, Haruki Sekikawa, Ai Inoue, Taiko Kanai, Hiroko Sarai, Akinori Ishii, Shunsuke Nishimura, Yoshifumi |
| description | The DNA-binding region of Myb consists of three imperfect tandem repeats (R1, R2, and R3). We have determined the solution structure of a specific DNA complex of the minimum DNA-binding domain (R2R3) by heteronuclear multidimensional NMR. Both R2 and R3 contain three helices, and the third helix in each is found to be a recognition helix. R2 and R3 are closely packed in the major groove, so that the two recognition helices contact each other directly to bind to the specific base sequence,
AA
CN
G cooperatively; this is a significant arrangement of recognition helices. The three key base pairs in this sequence are specifically recognized by Asn-183(R3), Lys-182(R3), and Lys-128 (R2). In contrast, R1 has no specific interactions with DNA from our NMR study of the DNA complex of the full DNA-binding domain (R1R2R3). |
| doi_str_mv | 10.1016/0092-8674(94)90549-5 |
| format | Article |
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AA
CN
G cooperatively; this is a significant arrangement of recognition helices. The three key base pairs in this sequence are specifically recognized by Asn-183(R3), Lys-182(R3), and Lys-128 (R2). In contrast, R1 has no specific interactions with DNA from our NMR study of the DNA complex of the full DNA-binding domain (R1R2R3).</description><identifier>ISSN: 0092-8674</identifier><identifier>EISSN: 1097-4172</identifier><identifier>DOI: 10.1016/0092-8674(94)90549-5</identifier><identifier>PMID: 7954830</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; Base Composition ; Binding Sites ; DNA - chemistry ; DNA - metabolism ; DNA-Binding Proteins - chemistry ; DNA-Binding Proteins - metabolism ; Drosophila - metabolism ; Humans ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oligodeoxyribonucleotides - chemistry ; Oligodeoxyribonucleotides - metabolism ; Protein Conformation ; Protein Structure, Secondary ; Proto-Oncogene Proteins - chemistry ; Proto-Oncogene Proteins - metabolism ; Proto-Oncogene Proteins c-myb ; Saccharomyces cerevisiae - metabolism ; Sequence Homology, Amino Acid ; Zea mays - metabolism ; Zinc Fingers</subject><ispartof>Cell, 1994-11, Vol.79 (4), p.639-648</ispartof><rights>1994</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c388t-ea768a61f5148321cfcfba0d783acb38331501cdf6bea483f0c00e7b7f5ab2d63</citedby><cites>FETCH-LOGICAL-c388t-ea768a61f5148321cfcfba0d783acb38331501cdf6bea483f0c00e7b7f5ab2d63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0092867494905495$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7954830$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ogata, Kazuhiro</creatorcontrib><creatorcontrib>Morikawa, Souichi</creatorcontrib><creatorcontrib>Nakamura, Haruki</creatorcontrib><creatorcontrib>Sekikawa, Ai</creatorcontrib><creatorcontrib>Inoue, Taiko</creatorcontrib><creatorcontrib>Kanai, Hiroko</creatorcontrib><creatorcontrib>Sarai, Akinori</creatorcontrib><creatorcontrib>Ishii, Shunsuke</creatorcontrib><creatorcontrib>Nishimura, Yoshifumi</creatorcontrib><title>Solution structure of a specific DNA complex of the Myb DNA-binding domain with cooperative recognition helices</title><title>Cell</title><addtitle>Cell</addtitle><description>The DNA-binding region of Myb consists of three imperfect tandem repeats (R1, R2, and R3). We have determined the solution structure of a specific DNA complex of the minimum DNA-binding domain (R2R3) by heteronuclear multidimensional NMR. Both R2 and R3 contain three helices, and the third helix in each is found to be a recognition helix. R2 and R3 are closely packed in the major groove, so that the two recognition helices contact each other directly to bind to the specific base sequence,
AA
CN
G cooperatively; this is a significant arrangement of recognition helices. The three key base pairs in this sequence are specifically recognized by Asn-183(R3), Lys-182(R3), and Lys-128 (R2). In contrast, R1 has no specific interactions with DNA from our NMR study of the DNA complex of the full DNA-binding domain (R1R2R3).</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Composition</subject><subject>Binding Sites</subject><subject>DNA - chemistry</subject><subject>DNA - metabolism</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Drosophila - metabolism</subject><subject>Humans</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Nucleic Acid Conformation</subject><subject>Oligodeoxyribonucleotides - chemistry</subject><subject>Oligodeoxyribonucleotides - metabolism</subject><subject>Protein Conformation</subject><subject>Protein Structure, Secondary</subject><subject>Proto-Oncogene Proteins - chemistry</subject><subject>Proto-Oncogene Proteins - metabolism</subject><subject>Proto-Oncogene Proteins c-myb</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>Zea mays - metabolism</subject><subject>Zinc Fingers</subject><issn>0092-8674</issn><issn>1097-4172</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUFPHSEUhYlpY5_Wf9AmrBpdjMJjgGFjYtS2JrZdtF0Thrn4aGaGERit_16m78WlTUhION89l5yD0AdKTimh4owQta4aIetjVZ8owmtV8T20okTJqqZy_QatXpB36CClP4SQhnO-j_al4nXDyAqFn6Gfsw8jTjnONs8RcHDY4DSB9c5bfPX9AtswTD38XZS8AfztqV2eq9aPnR_vcBcG40f86POmoGGCaLJ_ABzBhrvR_7PfQO8tpPforTN9gqPdfYh-f77-dfm1uv3x5eby4rayrGlyBUaKxgjqOC3_XFPrrGsN6WTDjG1ZwxjlhNrOiRZMIRyxhIBspeOmXXeCHaJPW98phvsZUtaDTxb63owQ5qSLPaFK1v8FqRCMCqYKWG9BG0NKEZyeoh9MfNKU6KUQvaStl7S1KmcpRPMy9nHnP7cDdC9DuwaKfr7VoaTx4CHqZD2MFjpf4su6C_71Bc8cjpti</recordid><startdate>19941118</startdate><enddate>19941118</enddate><creator>Ogata, Kazuhiro</creator><creator>Morikawa, Souichi</creator><creator>Nakamura, Haruki</creator><creator>Sekikawa, Ai</creator><creator>Inoue, Taiko</creator><creator>Kanai, Hiroko</creator><creator>Sarai, Akinori</creator><creator>Ishii, Shunsuke</creator><creator>Nishimura, Yoshifumi</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TM</scope><scope>7TO</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>19941118</creationdate><title>Solution structure of a specific DNA complex of the Myb DNA-binding domain with cooperative recognition helices</title><author>Ogata, Kazuhiro ; Morikawa, Souichi ; Nakamura, Haruki ; Sekikawa, Ai ; Inoue, Taiko ; Kanai, Hiroko ; Sarai, Akinori ; Ishii, Shunsuke ; Nishimura, Yoshifumi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c388t-ea768a61f5148321cfcfba0d783acb38331501cdf6bea483f0c00e7b7f5ab2d63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Composition</topic><topic>Binding Sites</topic><topic>DNA - chemistry</topic><topic>DNA - metabolism</topic><topic>DNA-Binding Proteins - chemistry</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Drosophila - metabolism</topic><topic>Humans</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Nucleic Acid Conformation</topic><topic>Oligodeoxyribonucleotides - chemistry</topic><topic>Oligodeoxyribonucleotides - metabolism</topic><topic>Protein Conformation</topic><topic>Protein Structure, Secondary</topic><topic>Proto-Oncogene Proteins - chemistry</topic><topic>Proto-Oncogene Proteins - metabolism</topic><topic>Proto-Oncogene Proteins c-myb</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><topic>Zea mays - metabolism</topic><topic>Zinc Fingers</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ogata, Kazuhiro</creatorcontrib><creatorcontrib>Morikawa, Souichi</creatorcontrib><creatorcontrib>Nakamura, Haruki</creatorcontrib><creatorcontrib>Sekikawa, Ai</creatorcontrib><creatorcontrib>Inoue, Taiko</creatorcontrib><creatorcontrib>Kanai, Hiroko</creatorcontrib><creatorcontrib>Sarai, Akinori</creatorcontrib><creatorcontrib>Ishii, Shunsuke</creatorcontrib><creatorcontrib>Nishimura, Yoshifumi</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ogata, Kazuhiro</au><au>Morikawa, Souichi</au><au>Nakamura, Haruki</au><au>Sekikawa, Ai</au><au>Inoue, Taiko</au><au>Kanai, Hiroko</au><au>Sarai, Akinori</au><au>Ishii, Shunsuke</au><au>Nishimura, Yoshifumi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Solution structure of a specific DNA complex of the Myb DNA-binding domain with cooperative recognition helices</atitle><jtitle>Cell</jtitle><addtitle>Cell</addtitle><date>1994-11-18</date><risdate>1994</risdate><volume>79</volume><issue>4</issue><spage>639</spage><epage>648</epage><pages>639-648</pages><issn>0092-8674</issn><eissn>1097-4172</eissn><abstract>The DNA-binding region of Myb consists of three imperfect tandem repeats (R1, R2, and R3). We have determined the solution structure of a specific DNA complex of the minimum DNA-binding domain (R2R3) by heteronuclear multidimensional NMR. Both R2 and R3 contain three helices, and the third helix in each is found to be a recognition helix. R2 and R3 are closely packed in the major groove, so that the two recognition helices contact each other directly to bind to the specific base sequence,
AA
CN
G cooperatively; this is a significant arrangement of recognition helices. The three key base pairs in this sequence are specifically recognized by Asn-183(R3), Lys-182(R3), and Lys-128 (R2). In contrast, R1 has no specific interactions with DNA from our NMR study of the DNA complex of the full DNA-binding domain (R1R2R3).</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>7954830</pmid><doi>10.1016/0092-8674(94)90549-5</doi><tpages>10</tpages></addata></record> |
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| ispartof | Cell, 1994-11, Vol.79 (4), p.639-648 |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Amino Acid Sequence Animals Base Composition Binding Sites DNA - chemistry DNA - metabolism DNA-Binding Proteins - chemistry DNA-Binding Proteins - metabolism Drosophila - metabolism Humans Magnetic Resonance Spectroscopy Models, Molecular Molecular Sequence Data Nucleic Acid Conformation Oligodeoxyribonucleotides - chemistry Oligodeoxyribonucleotides - metabolism Protein Conformation Protein Structure, Secondary Proto-Oncogene Proteins - chemistry Proto-Oncogene Proteins - metabolism Proto-Oncogene Proteins c-myb Saccharomyces cerevisiae - metabolism Sequence Homology, Amino Acid Zea mays - metabolism Zinc Fingers |
| title | Solution structure of a specific DNA complex of the Myb DNA-binding domain with cooperative recognition helices |
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