dc.contributor.author | Wolfram, F | |
dc.contributor.author | Morris, E | |
dc.contributor.author | Taylor, CW | |
dc.date.accessioned | 2018-06-05T09:03:56Z | |
dc.date.issued | 2010-05-27 | |
dc.identifier.citation | The Biochemical journal, 2010, 428 (3), pp. 483 - 489 | |
dc.identifier.issn | 0264-6021 | |
dc.identifier.uri | https://repository.icr.ac.uk/handle/internal/1702 | |
dc.identifier.eissn | 1470-8728 | |
dc.identifier.doi | 10.1042/bj20100143 | |
dc.description.abstract | IP3Rs (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. | |
dc.format | Electronic | |
dc.format.extent | 483 - 489 | |
dc.language | eng | |
dc.language.iso | eng | |
dc.publisher | PORTLAND PRESS LTD | |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0 | |
dc.subject | Cells, Cultured | |
dc.subject | Animals | |
dc.subject | Rats | |
dc.subject | Recombinant Proteins | |
dc.subject | Microscopy, Electron | |
dc.subject | Protein Conformation | |
dc.subject | Models, Molecular | |
dc.subject | Inositol 1,4,5-Trisphosphate Receptors | |
dc.title | Three-dimensional structure of recombinant type 1 inositol 1,4,5-trisphosphate receptor. | |
dc.type | Journal Article | |
rioxxterms.versionofrecord | 10.1042/bj20100143 | |
rioxxterms.licenseref.uri | https://creativecommons.org/licenses/by/4.0 | |
rioxxterms.licenseref.startdate | 2010-05-27 | |
rioxxterms.type | Journal Article/Review | |
dc.relation.isPartOf | The Biochemical journal | |
pubs.issue | 3 | |
pubs.notes | Not 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/Structural Biology | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions/Structural Biology/Structural Electron Microscopy | |
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.publication-status | Published | |
pubs.volume | 428 | |
pubs.embargo.terms | Not known | |
icr.researchteam | Structural Electron Microscopy | |
dc.contributor.icrauthor | Morris, Edward | |