Native mass spectrometry of calmodulin binding to the plasma-membrane Ca2+-ATPase ACA8
Ontology highlight
ABSTRACT:
INSTRUMENT(S): Q-Tof ultima
ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)
SUBMITTER: 
Johannes Heidemann
LAB HEAD: Charlotte Uetrecht
PROVIDER: PXD011177 | Pride | 2018-12-05
REPOSITORIES: Pride
Dataset's files
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| 20150929J048_80_raw.txt | Txt | |||
| 20150929J048_80sm2x3.txt | Txt | |||
| 20150929J048_80sm2x3_fig.PNG | Other | |||
| 20150929J048_80sm2x3_settings.txt | Txt | |||
| 20150929J0542_174sm2x20.PNG | Other |
Items per page: 5 1 - 5 of 32 |
Publications
Structural basis for activation of plasma-membrane Ca<sup>2+</sup>-ATPase by calmodulin.
Nitsche Julius J Josts Inokentijs I Heidemann Johannes J Mertens Haydyn D HD Maric Selma S Moulin Martine M Haertlein Michael M Busch Sebastian S Forsyth V Trevor VT Svergun Dmitri I DI Uetrecht Charlotte C Tidow Henning H
Communications biology 20181126
Plasma-membrane Ca<sup>2+</sup>-ATPases expel Ca<sup>2+</sup> from the cytoplasm and are key regulators of Ca<sup>2+</sup> homeostasis in eukaryotes. They are autoinhibited under low Ca<sup>2+</sup> concentrations. Calmodulin (CaM)-binding to a unique regulatory domain releases the autoinhibition and activates the pump. However, the structural basis for this activation, including the overall structure of this calcium pump and its complex with calmodulin, is unknown. We previously determined the ...[more]
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