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dc.contributor.authorOliver, AW
dc.contributor.authorJones, SA
dc.contributor.authorRoe, SM
dc.contributor.authorMatthews, S
dc.contributor.authorGoodwin, GH
dc.contributor.authorPearl, LH
dc.date.accessioned2018-09-07T09:07:27Z
dc.date.issued2005-08
dc.identifier.citationThe Biochemical journal, 2005, 389 (Pt 3), pp. 657 - 664
dc.identifier.issn0264-6021
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/2592
dc.identifier.eissn1470-8728
dc.identifier.doi10.1042/bj20050310
dc.description.abstractThe BAH domain (bromo-associated homology domain) was first identified from a repeated motif found in the nuclear protein polybromo--a large (187 kDa) modular protein comprising six bromodomains, two BAH domains and an HMG box. To date, the BAH domain has no ascribed function, although it is found in a wide range of proteins that contain additional domains involved in either transcriptional regulation (e.g. SET, PHD and bromodomain) and/or DNA binding (HMG box and AT hook). The molecular function of polybromo itself also remains unclear, but it has been identified as a key component of an SWI/SNF (switching/sucrose non-fermenting)-related, ATP-dependent chromatin-remodelling complex PBAF (polybromo, BRG1-associated factors; also known as SWI/SNF-B or SWI/SNFbeta). We present in this paper the crystal structure of the proximal BAH domain from chicken polybromo (BAH1), at a resolution of 1.6 A (1 A=0.1 nm). Structure-based sequence analysis reveals several features that may be involved in mediating protein-protein interactions.
dc.formatPrint
dc.format.extent657 - 664
dc.languageeng
dc.language.isoeng
dc.subjectAnimals
dc.subjectChickens
dc.subjectNuclear Proteins
dc.subjectTranscription Factors
dc.subjectCrystallization
dc.subjectSequence Alignment
dc.subjectAmino Acid Sequence
dc.subjectConserved Sequence
dc.subjectProtein Structure, Tertiary
dc.subjectSequence Homology, Amino Acid
dc.subjectMolecular Sequence Data
dc.titleCrystal structure of the proximal BAH domain of the polybromo protein.
dc.typeJournal Article
rioxxterms.versionofrecord10.1042/bj20050310
rioxxterms.licenseref.startdate2005-08
rioxxterms.typeJournal Article/Review
dc.relation.isPartOfThe Biochemical journal
pubs.issuePt 3
pubs.notesNot known
pubs.organisational-group/ICR
pubs.organisational-group/ICR
pubs.publication-statusPublished
pubs.volume389
pubs.embargo.termsNot known
dc.contributor.icrauthorPearl, Laurenceen


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