Crystal structure of Na+, K(+)-ATPase in the Na(+)-bound state (Q27686727)

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Pontus Gourdon

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Magnus Andersson

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Natalya Fedosova

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Poul Nissen

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author name string

Hanne Poulsen

2

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Linda Reinhard

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Erik Lindahl

6

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language of work or name

English

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publication date

4 October 2013

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published in

Science

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volume

342

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page(s)

123-127

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issue

6154

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Crystal structure of the sodium–potassium pump

14 June 2020

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Crystal structure of the sodium-potassium pump at 2.4 A resolution

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Crystal structure of the sodium-potassium pump (Na+,K+-ATPase) with bound potassium and ouabain

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The sarcolipin-bound calcium pump stabilizes calcium sites exposed to the cytoplasm

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The rapid-onset dystonia parkinsonism mutation D923N of the Na+, K+-ATPase alpha3 isoform disrupts Na+ interaction at the third Na+ site

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Hyperpolarization-activated inward leakage currents caused by deletion or mutation of carboxy-terminal tyrosines of the Na+/K+-ATPase {alpha} subunit

21 January 2018

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The two C-terminal tyrosines stabilize occluded Na/K pump conformations containing Na or K ions

21 January 2018

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The C terminus of Na+,K+-ATPase controls Na+ affinity on both sides of the membrane through Arg935.

21 January 2018

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A C-terminal mutation of ATP1A3 underscores the crucial role of sodium affinity in the pathophysiology of rapid-onset dystonia-parkinsonism

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Thr-774 (transmembrane segment M5), Val-920 (M8), and Glu-954 (M9) are involved in Na+ transport, and Gln-923 (M8) is essential for Na,K-ATPase activity

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21 January 2018

Identifiers

DOI

10.1126/SCIENCE.1243352

2 references

Consolidated OpenCitations Corpus – April 2017

640229

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14 June 2020

640229

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

2 references

640229