Crystal structure of a complex of DNA with one AT-hook of HMGA1
We present here for the first time the crystal structure of an AT-hook domain. We show the structure of an AT-hook of the ubiquitous nuclear protein HMGA1, combined with the oligonucleotide d(CGAATTAATTCG)(2), which has two potential AATT interacting groups. Interaction with only one of them is foun...
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| Veröffentlicht in: | PloS one 2012-05, Vol.7 (5), p.e37120-e37120 |
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| creator | Fonfría-Subirós, Elsa Acosta-Reyes, Francisco Saperas, Núria Pous, Joan Subirana, Juan A Campos, J Lourdes |
| description | We present here for the first time the crystal structure of an AT-hook domain. We show the structure of an AT-hook of the ubiquitous nuclear protein HMGA1, combined with the oligonucleotide d(CGAATTAATTCG)(2), which has two potential AATT interacting groups. Interaction with only one of them is found. The structure presents analogies and significant differences with previous NMR studies: the AT-hook forms hydrogen bonds between main-chain NH groups and thymines in the minor groove, DNA is bent and the minor groove is widened. |
| doi_str_mv | 10.1371/journal.pone.0037120 |
| format | Article |
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We show the structure of an AT-hook of the ubiquitous nuclear protein HMGA1, combined with the oligonucleotide d(CGAATTAATTCG)(2), which has two potential AATT interacting groups. Interaction with only one of them is found. The structure presents analogies and significant differences with previous NMR studies: the AT-hook forms hydrogen bonds between main-chain NH groups and thymines in the minor groove, DNA is bent and the minor groove is widened.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0037120</identifier><identifier>PMID: 22615915</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>ADN ; Amino acids ; Apoptosis ; Automation ; Binding Sites ; Biochemistry ; Biology ; Chromosomal proteins ; Cristal·lografia ; Crystal structure ; Crystallography, X-Ray - methods ; Deoxyribonucleic acid ; DNA ; DNA - chemistry ; DNA - metabolism ; DNA binding proteins ; DNA methylation ; Enginyeria química ; Geometry ; HMGA Proteins - chemistry ; HMGA Proteins - metabolism ; Hydration ; Hydrogen ; Hydrogen Bonding ; Hydrogen bonds ; Magnetic Resonance Spectroscopy - methods ; Mass spectrometry ; Models, Molecular ; NMR ; Nuclear magnetic resonance ; Oligonucleotides ; Oligonucleotides - metabolism ; Packaging ; Peptides ; Phosphates ; Protein Structure, Tertiary ; Proteins ; Scientific imaging ; Software packages ; Transcription (Genetics) ; Type 2 diabetes ; Àrees temàtiques de la UPC</subject><ispartof>PloS one, 2012-05, Vol.7 (5), p.e37120-e37120</ispartof><rights>COPYRIGHT 2012 Public Library of Science</rights><rights>2012 Fonfría-Subirós et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>Attribution-NonCommercial-NoDerivs 3.0 Spain info:eu-repo/semantics/openAccess <a href="http://creativecommons.org/licenses/by-nc-nd/3.0/es/">http://creativecommons.org/licenses/by-nc-nd/3.0/es/</a></rights><rights>Fonfría-Subirós et al. 2012</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c734t-4822d893534590bd47e9196961927e601f78fb7724eb1b37e650452c7b47f85b3</citedby><cites>FETCH-LOGICAL-c734t-4822d893534590bd47e9196961927e601f78fb7724eb1b37e650452c7b47f85b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3353895/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3353895/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2096,2915,23845,26951,27901,27902,53766,53768,79342,79343</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22615915$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fonfría-Subirós, Elsa</creatorcontrib><creatorcontrib>Acosta-Reyes, Francisco</creatorcontrib><creatorcontrib>Saperas, Núria</creatorcontrib><creatorcontrib>Pous, Joan</creatorcontrib><creatorcontrib>Subirana, Juan A</creatorcontrib><creatorcontrib>Campos, J Lourdes</creatorcontrib><title>Crystal structure of a complex of DNA with one AT-hook of HMGA1</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>We present here for the first time the crystal structure of an AT-hook domain. We show the structure of an AT-hook of the ubiquitous nuclear protein HMGA1, combined with the oligonucleotide d(CGAATTAATTCG)(2), which has two potential AATT interacting groups. Interaction with only one of them is found. The structure presents analogies and significant differences with previous NMR studies: the AT-hook forms hydrogen bonds between main-chain NH groups and thymines in the minor groove, DNA is bent and the minor groove is widened.</description><subject>ADN</subject><subject>Amino acids</subject><subject>Apoptosis</subject><subject>Automation</subject><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Biology</subject><subject>Chromosomal proteins</subject><subject>Cristal·lografia</subject><subject>Crystal structure</subject><subject>Crystallography, X-Ray - methods</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA - chemistry</subject><subject>DNA - metabolism</subject><subject>DNA binding proteins</subject><subject>DNA methylation</subject><subject>Enginyeria química</subject><subject>Geometry</subject><subject>HMGA Proteins - chemistry</subject><subject>HMGA Proteins - metabolism</subject><subject>Hydration</subject><subject>Hydrogen</subject><subject>Hydrogen Bonding</subject><subject>Hydrogen bonds</subject><subject>Magnetic Resonance Spectroscopy - 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We show the structure of an AT-hook of the ubiquitous nuclear protein HMGA1, combined with the oligonucleotide d(CGAATTAATTCG)(2), which has two potential AATT interacting groups. Interaction with only one of them is found. The structure presents analogies and significant differences with previous NMR studies: the AT-hook forms hydrogen bonds between main-chain NH groups and thymines in the minor groove, DNA is bent and the minor groove is widened.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>22615915</pmid><doi>10.1371/journal.pone.0037120</doi><tpages>e37120</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | ADN Amino acids Apoptosis Automation Binding Sites Biochemistry Biology Chromosomal proteins Cristal·lografia Crystal structure Crystallography, X-Ray - methods Deoxyribonucleic acid DNA DNA - chemistry DNA - metabolism DNA binding proteins DNA methylation Enginyeria química Geometry HMGA Proteins - chemistry HMGA Proteins - metabolism Hydration Hydrogen Hydrogen Bonding Hydrogen bonds Magnetic Resonance Spectroscopy - methods Mass spectrometry Models, Molecular NMR Nuclear magnetic resonance Oligonucleotides Oligonucleotides - metabolism Packaging Peptides Phosphates Protein Structure, Tertiary Proteins Scientific imaging Software packages Transcription (Genetics) Type 2 diabetes Àrees temàtiques de la UPC |
| title | Crystal structure of a complex of DNA with one AT-hook of HMGA1 |
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