Mostra el registre d'ítem simple

dc.contributor.authorSánchez Giraldo, Raquel
dc.contributor.authorAcosta Reyes, Francisco Javier
dc.contributor.authorMalarkey, Christopher S.
dc.contributor.authorSaperas Plana, Núria
dc.contributor.authorChurchill, Mair E. A.
dc.contributor.authorCampos López, Josefina de Lourdes
dc.contributor.otherUniversitat Politècnica de Catalunya. Departament d'Enginyeria Química
dc.date.accessioned2015-10-22T10:34:56Z
dc.date.available2015-10-22T10:34:56Z
dc.date.issued2015-07-02
dc.identifier.citationSanchez, R., Acosta, F.J., Malarkey, C.S., Saperas, N., Churchill, M.E.A., Campos, J.Lourdes. Two high-mobility group box domains act together to underwind and kink DNA.. "Acta crystallographica. Section D, biological crystallography", 02 Juliol 2015, vol. D71, núm. part 7, p. 1423-1432.
dc.identifier.issn0907-4449
dc.identifier.urihttp://hdl.handle.net/2117/78117
dc.description.abstractHigh-mobility group protein 1 (HMGB1) is an essential and ubiquitous DNA architectural factor that influences a myriad of cellular processes. HMGB1 contains two DNA-binding domains, box A and box B, which have little sequence specificity but have remarkable abilities to underwind and bend DNA. Although HMGB1 box A is thought to be responsible for the majority of HMGB1-DNA interactions with pre-bent or kinked DNA, little is known about how it recognizes unmodified DNA. Here, the crystal structure of HMGB1 box A bound to an AT-rich DNA fragment is reported at a resolution of 2 angstrom. Two box A domains of HMGB1 collaborate in an unusual configuration in which the Phe37 residues of both domains stack together and intercalate the same CG base pair, generating highly kinked DNA. This represents a novel mode of DNA recognition for HMGB proteins and reveals a mechanism by which structure-specific HMG boxes kink linear DNA.
dc.format.extent10 p.
dc.language.isoeng
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/es/
dc.subjectÀrees temàtiques de la UPC::Enginyeria química
dc.subject.lcshDNA-protein interactions
dc.subject.otherHigh-mobility group protein
dc.subject.otherX-ray crystallography
dc.subject.otherDNA binding
dc.subject.otherhmgb1
dc.subject.othercisplatin-modified dna
dc.subject.othermitochondrial transcription factor
dc.subject.other4-way junction dna
dc.subject.othertandem hmg boxes
dc.subject.otherintercalating residues
dc.subject.otherbinding proteins
dc.subject.otherhistone h1
dc.subject.otherduplex dna
dc.subject.othera-domain
dc.subject.otherchromatin
dc.titleTwo high-mobility group box domains act together to underwind and kink DNA.
dc.typeArticle
dc.subject.lemacADN -- Interaccions de les proteïnes
dc.contributor.groupUniversitat Politècnica de Catalunya. MACROM - Cristal·lografia, Estructura i Funció de Macromolècules Biològiques
dc.identifier.doi10.1107/S1399004715007452
dc.description.peerreviewedPeer Reviewed
dc.relation.publisherversionhttp://journals.iucr.org/d/issues/2015/07/00/mh5175/mh5175.pdf
dc.rights.accessOpen Access
drac.iddocument16650919
dc.description.versionPostprint (published version)
upcommons.citation.authorSanchez, R., Acosta, F.J., Malarkey, C.S., Saperas, N., Churchill, M.E.A., Campos, J.Lourdes
upcommons.citation.publishedtrue
upcommons.citation.publicationNameActa crystallographica. Section D, biological crystallography
upcommons.citation.volumeD71
upcommons.citation.numberpart 7
upcommons.citation.startingPage1423
upcommons.citation.endingPage1432


Fitxers d'aquest items

Thumbnail

Aquest ítem apareix a les col·leccions següents

Mostra el registre d'ítem simple

Llevat que s'hi indiqui el contrari, els continguts d'aquesta obra estan subjectes a la llicència de Creative Commons: Reconeixement-NoComercial-SenseObraDerivada 3.0 Espanya