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Sequential substitution of K+ bound to Na+,K+-ATPase visualized by X-ray crystallography

Sequential substitution of K+ bound to Na+,K+-ATPase visualized by X-ray crystallography

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4918401

Sequential substitution of K+ bound to Na+,K+-ATPase visualized by X-ray crystallography

About this item

Full title

Sequential substitution of K+ bound to Na+,K+-ATPase visualized by X-ray crystallography

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2015-08, Vol.6 (1), p.8004-8004, Article 8004

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Na
+
,K
+
-ATPase transfers three Na
+
from the cytoplasm into the extracellular medium and two K
+
in the opposite direction per ATP hydrolysed. The binding and release of Na
+
and K
+
are all thought to occur sequentially. Here we demonstrate by X-ray crystallography of the ATPase in E2·MgF
4
2−
·2K

Alternative Titles

Full title

Sequential substitution of K+ bound to Na+,K+-ATPase visualized by X-ray crystallography

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4918401

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4918401

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/ncomms9004

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