Show simple item record

dc.contributor.authorLlorca, O
dc.contributor.authorRivera-Calzada, A
dc.contributor.authorGrantham, J
dc.contributor.authorWillison, KR
dc.date.accessioned2018-09-12T14:15:26Z
dc.date.issued2003-06-19
dc.identifier25
dc.identifier.citationONCOGENE, 2003, 22 pp. 3867 - 3874
dc.identifier.issn0950-9232
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/2667
dc.identifier.doi10.1038/sj.onc.1206649
dc.description.abstractThe human tumor suppressor gene ataxia telangiectasia mutated (ATM) encodes a 3056 amino-acid protein kinase that regulates cell cycle checkpoints. ATM is defective in the neurodegenerative and cancer predisposition syndrome ataxia-telangiectasia. ATM protein kinase is activated by DNA damage and responds by phosphorylating downstream effectors involved in cell cycle arrest and DNA repair, such as p53, MDM2, CHEK2, BRCA1 and H2AX. ATM is probably a component of, or in close proximity to, the double-stranded DNA break-sensing machinery. We have observed purified human ATM protein, ATM-DNA and ATM-DNA-avidin bound complexes by single-particle electron microscopy and obtained three-dimensional reconstructions which show that ATM is composed of two main domains comprising a head and an arm. DNA binding to ATM induces a large conformational movement of the arm-like domain. Taken together, these three structures suggest that ATM is capable of interacting with DNA, using its arm to clamp around the double helix.
dc.format.extent3867 - 3874
dc.languageeng
dc.language.isoeng
dc.titleElectron microscopy and 3D reconstructions reveal that human ATM kinase uses an arm-like domain to clamp around double-stranded DNA
dc.typeJournal Article
rioxxterms.versionofrecord10.1038/sj.onc.1206649
rioxxterms.licenseref.startdate2003-06-19
rioxxterms.typeJournal Article/Review
dc.relation.isPartOfONCOGENE
pubs.notesresearcherid-numbers: Llorca, Oscar/K-1144-2014 Grantham, Julie/A-5002-2009 orcid-numbers: Llorca, Oscar/0000-0001-5705-0699 unique-id: ISI:000183612000006
pubs.notesNot known
pubs.organisational-group/ICR
pubs.organisational-group/ICR/Primary Group
pubs.organisational-group/ICR/Primary Group/ICR Divisions
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Closed research teams
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Closed research teams/Chromatin Regulation
pubs.organisational-group/ICR
pubs.organisational-group/ICR/Primary Group
pubs.organisational-group/ICR/Primary Group/ICR Divisions
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Closed research teams
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Closed research teams/Chromatin Regulation
pubs.volume22en_US
pubs.embargo.termsNot known
icr.researchteamChromatin Regulationen_US
dc.contributor.icrauthorWillison, Keithen


Files in this item

FilesSizeFormatView

There are no files associated with this item.

This item appears in the following collection(s)

Show simple item record