Design and synthesis of BRC analogous peptides and their interactions with a key p53 peptide
Mutations in breast cancer susceptibility gene 2 (BRCA2) can lead to chromosomal instability and result in breast cancer, which is strongly associated with p53 mutations. Here, based on the crystal structure of BRC4 and p53, the spatial structure of BRC2 and p53 (171–192) was simulated, providing st...
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| Veröffentlicht in: | FEBS letters 2018-10, Vol.592 (20), p.3438-3445 |
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| creator | Zhao, Dongxin Lu, Kui Liu, Guangbin Ma, Li Zhu, Hanjing He, Juan |
| description | Mutations in breast cancer susceptibility gene 2 (BRCA2) can lead to chromosomal instability and result in breast cancer, which is strongly associated with p53 mutations. Here, based on the crystal structure of BRC4 and p53, the spatial structure of BRC2 and p53 (171–192) was simulated, providing structural basis for the site‐specific mutation of BRC2. The BRC analogous peptides and p53 (171–192) were synthesized, and the interaction between the mutant peptide and p53 (171–192) was studied using circular diachronic spectroscopy and fluorescence spectroscopy. The results show that the mutations of amino acid residues constituting the BRC2 α‐helix significantly affect the structure and interaction of BRC analogs and p53 (171–192), which provides support for understanding the structure of the BRC repeat motifs and its interaction pattern with p53. |
| doi_str_mv | 10.1002/1873-3468.13256 |
| format | Article |
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Here, based on the crystal structure of BRC4 and p53, the spatial structure of BRC2 and p53 (171–192) was simulated, providing structural basis for the site‐specific mutation of BRC2. The BRC analogous peptides and p53 (171–192) were synthesized, and the interaction between the mutant peptide and p53 (171–192) was studied using circular diachronic spectroscopy and fluorescence spectroscopy. The results show that the mutations of amino acid residues constituting the BRC2 α‐helix significantly affect the structure and interaction of BRC analogs and p53 (171–192), which provides support for understanding the structure of the BRC repeat motifs and its interaction pattern with p53.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1002/1873-3468.13256</identifier><identifier>PMID: 30238447</identifier><language>eng</language><publisher>England</publisher><subject>Amino Acid Motifs ; analogous peptide ; Binding Sites - genetics ; BRC repeat motifs ; BRCA2 Protein - chemistry ; BRCA2 Protein - genetics ; BRCA2 Protein - metabolism ; Circular Dichroism ; Crystallography, X-Ray ; homologous modeling ; Humans ; Models, Molecular ; Mutation ; Peptides - chemical synthesis ; Peptides - genetics ; Peptides - metabolism ; Protein Binding ; Spectrometry, Fluorescence ; tumor suppressor ; Tumor Suppressor Protein p53 - chemistry ; Tumor Suppressor Protein p53 - genetics ; Tumor Suppressor Protein p53 - metabolism</subject><ispartof>FEBS letters, 2018-10, Vol.592 (20), p.3438-3445</ispartof><rights>2018 Federation of European Biochemical Societies</rights><rights>2018 Federation of European Biochemical Societies.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3856-1d141b19ee4719fe88d4ee1b65ce28fc2051016a903e7c4533b8edd67d703ed73</citedby><cites>FETCH-LOGICAL-c3856-1d141b19ee4719fe88d4ee1b65ce28fc2051016a903e7c4533b8edd67d703ed73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2F1873-3468.13256$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2F1873-3468.13256$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,1427,27901,27902,45550,45551,46384,46808</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/30238447$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhao, Dongxin</creatorcontrib><creatorcontrib>Lu, Kui</creatorcontrib><creatorcontrib>Liu, Guangbin</creatorcontrib><creatorcontrib>Ma, Li</creatorcontrib><creatorcontrib>Zhu, Hanjing</creatorcontrib><creatorcontrib>He, Juan</creatorcontrib><title>Design and synthesis of BRC analogous peptides and their interactions with a key p53 peptide</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Mutations in breast cancer susceptibility gene 2 (BRCA2) can lead to chromosomal instability and result in breast cancer, which is strongly associated with p53 mutations. Here, based on the crystal structure of BRC4 and p53, the spatial structure of BRC2 and p53 (171–192) was simulated, providing structural basis for the site‐specific mutation of BRC2. The BRC analogous peptides and p53 (171–192) were synthesized, and the interaction between the mutant peptide and p53 (171–192) was studied using circular diachronic spectroscopy and fluorescence spectroscopy. The results show that the mutations of amino acid residues constituting the BRC2 α‐helix significantly affect the structure and interaction of BRC analogs and p53 (171–192), which provides support for understanding the structure of the BRC repeat motifs and its interaction pattern with p53.</description><subject>Amino Acid Motifs</subject><subject>analogous peptide</subject><subject>Binding Sites - genetics</subject><subject>BRC repeat motifs</subject><subject>BRCA2 Protein - chemistry</subject><subject>BRCA2 Protein - genetics</subject><subject>BRCA2 Protein - metabolism</subject><subject>Circular Dichroism</subject><subject>Crystallography, X-Ray</subject><subject>homologous modeling</subject><subject>Humans</subject><subject>Models, Molecular</subject><subject>Mutation</subject><subject>Peptides - chemical synthesis</subject><subject>Peptides - genetics</subject><subject>Peptides - metabolism</subject><subject>Protein Binding</subject><subject>Spectrometry, Fluorescence</subject><subject>tumor suppressor</subject><subject>Tumor Suppressor Protein p53 - chemistry</subject><subject>Tumor Suppressor Protein p53 - genetics</subject><subject>Tumor Suppressor Protein p53 - metabolism</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMFLwzAUh4Mobk7P3iRHL93ymjRJjzqdCoIgehNC27zOaNfWpkP235utuqvvEt6P7_0IHyHnwKbAWDwDrXjEhdRT4HEiD8h4nxySMWMgokSlfEROvP9gYdeQHpMRZzHXQqgxebtB75Y1zWpL_abu38PqaVPS6-d5CLOqWTZrT1tse2fR77gAuY66uscuK3rX1J5-u_6dZvQTN7RN-B9-So7KrPJ49vtOyOvi9mV-Hz0-3T3Mrx6jgutERmBBQA4polCQlqi1FYiQy6TAWJdFzBJgILOUcVSFSDjPNVorlVUhsYpPyOXQ23bN1xp9b1bOF1hVWY3h9yaGMEIqkAGdDWjRNd53WJq2c6us2xhgZqvUbAWarUCzUxouLn7L1_kK7Z7_cxgAOQDfrsLNf31mcXsdD80_ZOp_0A</recordid><startdate>201810</startdate><enddate>201810</enddate><creator>Zhao, Dongxin</creator><creator>Lu, Kui</creator><creator>Liu, Guangbin</creator><creator>Ma, Li</creator><creator>Zhu, Hanjing</creator><creator>He, Juan</creator><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>7X8</scope></search><sort><creationdate>201810</creationdate><title>Design and synthesis of BRC analogous peptides and their interactions with a key p53 peptide</title><author>Zhao, Dongxin ; Lu, Kui ; Liu, Guangbin ; Ma, Li ; Zhu, Hanjing ; He, Juan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3856-1d141b19ee4719fe88d4ee1b65ce28fc2051016a903e7c4533b8edd67d703ed73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Amino Acid Motifs</topic><topic>analogous peptide</topic><topic>Binding Sites - genetics</topic><topic>BRC repeat motifs</topic><topic>BRCA2 Protein - chemistry</topic><topic>BRCA2 Protein - genetics</topic><topic>BRCA2 Protein - metabolism</topic><topic>Circular Dichroism</topic><topic>Crystallography, X-Ray</topic><topic>homologous modeling</topic><topic>Humans</topic><topic>Models, Molecular</topic><topic>Mutation</topic><topic>Peptides - chemical synthesis</topic><topic>Peptides - genetics</topic><topic>Peptides - metabolism</topic><topic>Protein Binding</topic><topic>Spectrometry, Fluorescence</topic><topic>tumor suppressor</topic><topic>Tumor Suppressor Protein p53 - chemistry</topic><topic>Tumor Suppressor Protein p53 - genetics</topic><topic>Tumor Suppressor Protein p53 - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhao, Dongxin</creatorcontrib><creatorcontrib>Lu, Kui</creatorcontrib><creatorcontrib>Liu, Guangbin</creatorcontrib><creatorcontrib>Ma, Li</creatorcontrib><creatorcontrib>Zhu, Hanjing</creatorcontrib><creatorcontrib>He, Juan</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhao, Dongxin</au><au>Lu, Kui</au><au>Liu, Guangbin</au><au>Ma, Li</au><au>Zhu, Hanjing</au><au>He, Juan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Design and synthesis of BRC analogous peptides and their interactions with a key p53 peptide</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2018-10</date><risdate>2018</risdate><volume>592</volume><issue>20</issue><spage>3438</spage><epage>3445</epage><pages>3438-3445</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Mutations in breast cancer susceptibility gene 2 (BRCA2) can lead to chromosomal instability and result in breast cancer, which is strongly associated with p53 mutations. Here, based on the crystal structure of BRC4 and p53, the spatial structure of BRC2 and p53 (171–192) was simulated, providing structural basis for the site‐specific mutation of BRC2. The BRC analogous peptides and p53 (171–192) were synthesized, and the interaction between the mutant peptide and p53 (171–192) was studied using circular diachronic spectroscopy and fluorescence spectroscopy. The results show that the mutations of amino acid residues constituting the BRC2 α‐helix significantly affect the structure and interaction of BRC analogs and p53 (171–192), which provides support for understanding the structure of the BRC repeat motifs and its interaction pattern with p53.</abstract><cop>England</cop><pmid>30238447</pmid><doi>10.1002/1873-3468.13256</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| source | Wiley Free Content; MEDLINE; Wiley Online Library Journals Frontfile Complete; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Amino Acid Motifs analogous peptide Binding Sites - genetics BRC repeat motifs BRCA2 Protein - chemistry BRCA2 Protein - genetics BRCA2 Protein - metabolism Circular Dichroism Crystallography, X-Ray homologous modeling Humans Models, Molecular Mutation Peptides - chemical synthesis Peptides - genetics Peptides - metabolism Protein Binding Spectrometry, Fluorescence tumor suppressor Tumor Suppressor Protein p53 - chemistry Tumor Suppressor Protein p53 - genetics Tumor Suppressor Protein p53 - metabolism |
| title | Design and synthesis of BRC analogous peptides and their interactions with a key p53 peptide |
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