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Full-length Gαq–phospholipase C-β3 structure reveals interfaces of the C-terminal coiled-coil domain

Full-length Gαq–phospholipase C-β3 structure reveals interfaces of the C-terminal coiled-coil domain

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3594540

Full-length Gαq–phospholipase C-β3 structure reveals interfaces of the C-terminal coiled-coil domain

About this item

Full title

Full-length Gαq–phospholipase C-β3 structure reveals interfaces of the C-terminal coiled-coil domain

Publisher

New York: Nature Publishing Group US

Journal title

Nature structural & molecular biology, 2013-03, Vol.20 (3), p.355-362

Language

English

Formats

Publication information

Publisher

New York: Nature Publishing Group US

More information

Scope and Contents

Contents

The regulatory importance of the C-terminal coiled-coil domain of PLCβ has long been known yet remains poorly understood. The crystal structure and cryo-EM reconstruction of full-length PLCβ3 bound to its activator Gα
q
reveals that the C terminus makes contact with both the catalytic core and Gα
q
to contribute to the complex regulatio...

Alternative Titles

Full title

Full-length Gαq–phospholipase C-β3 structure reveals interfaces of the C-terminal coiled-coil domain

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3594540

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3594540

Other Identifiers

ISSN

1545-9993

E-ISSN

1545-9985

DOI

10.1038/nsmb.2497

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