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dc.contributor.authorWolfram, Fen_US
dc.contributor.authorMorris, Een_US
dc.contributor.authorTaylor, CWen_US
dc.date.accessioned2018-06-05T09:03:56Z
dc.date.issued2010-06en_US
dc.identifier.citationThe Biochemical journal, 2010, 428 (3), pp. 483 - 489en_US
dc.identifier.issn0264-6021en_US
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/1702
dc.identifier.eissn1470-8728en_US
dc.identifier.doi10.1042/bj20100143en_US
dc.description.abstractIP3Rs (inositol 1,4,5-trisphosphate receptors) are the intracellular channels that mediate release of Ca2+ from the endoplasmic reticulum in response to the many stimuli that evoke Ins(1,4,5)P3 formation. We characterized and purified type 1 IP3R heterologously expressed in Sf9 insect cells, and used the purified IP3R1 to determine its three-dimensional structure by electron microscopy and single-particle analysis. Recombinant IP3R1 has 4-fold symmetry with overall dimensions of approx. 19.5 nm x 19.5 nm x 17.5 nm. It comprises a small domain, which is likely to include the pore, linked by slender bridges to a large cytoplasmic domain with four petal-like regions. Our structures of recombinant IP3R1 and native cerebellar IP3R have similar appearances and dimensions. The only notable difference is the absence of a central stigma-like domain from the cytoplasmic region of recombinant IP3R1. The first structure of a recombinant IP3R is an important step towards developing three-dimensional structures of IP3R that better contribute to our understanding of the structural basis of IP3R activation.en_US
dc.formatElectronicen_US
dc.format.extent483 - 489en_US
dc.languageengen_US
dc.language.isoengen_US
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en_US
dc.subjectCells, Cultureden_US
dc.subjectAnimalsen_US
dc.subjectRatsen_US
dc.subjectRecombinant Proteinsen_US
dc.subjectMicroscopy, Electronen_US
dc.subjectProtein Conformationen_US
dc.subjectModels, Molecularen_US
dc.subjectInositol 1,4,5-Trisphosphate Receptorsen_US
dc.titleThree-dimensional structure of recombinant type 1 inositol 1,4,5-trisphosphate receptor.en_US
dc.typeJournal Article
rioxxterms.versionofrecord10.1042/bj20100143en_US
rioxxterms.licenseref.startdate2010-06en_US
rioxxterms.typeJournal Article/Reviewen_US
dc.relation.isPartOfThe Biochemical journalen_US
pubs.issue3en_US
pubs.notesNot knownen_US
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/Structural Biology
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Structural Biology/Structural Electron Microscopy
pubs.volume428en_US
pubs.embargo.termsNot knownen_US
icr.researchteamStructural Electron Microscopyen_US
dc.contributor.icrauthorMorris, Edwarden_US


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