The Crystallographic Structure of Na,K-ATPase N-domain at 2.6Å Resolution (Q27642194)

https://api.crossref.org/works/10.1016/J.JMB.2003.07.012

11 March 2024

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https://api.crossref.org/works/10.1016/J.JMB.2003.07.012

11 March 2024

author name string

Kjell O. Håkansson

1

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Europe PubMed Central

PubMed ID

14499619

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A14499619

full work available at URL

11 March 2024

language of work or name

English

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publication date

3 October 2003

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https://api.elsevier.com/content/article/PII:S0022283603009938?httpAccept=text/xml

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https://api.crossref.org/works/10.1016/J.JMB.2003.07.012

https://api.elsevier.com/content/article/PII:S0022283603009938?httpAccept=text/plain

11 March 2024

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https://api.crossref.org/works/10.1016/J.JMB.2003.07.012

Journal of Molecular Biology

11 March 2024

published in

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volume

332

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issue

5

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page(s)

1175-82

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cites work

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Structure and mechanism of Na,K-ATPase: functional sites and their interactions

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Structural basis for E1-E2 conformational transitions in Na,K-pump and Ca-pump proteins

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Purification and characterization of (Na+, K+)-ATPase. V. Conformational changes in the enzyme. Transitions between the Na-form and the K-form studied with tryptic digestion as a tool

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Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution

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Structural changes in the calcium pump accompanying the dissociation of calcium

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Ultrastructure of the sodium pump: Comparison of thin sectioning, negative staining, and freeze-fracture of purified, membrane-bound (Na+, K+)-ATPase

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Three-dimensional structure of renal Na,K-ATPase from cryo-electron microscopy of two-dimensional crystals

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A structural model for the catalytic cycle of Ca(2+)-ATPase

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Structure of Na+,K+-ATPase at 11-A resolution: comparison with Ca2+-ATPase in E1 and E2 states

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Identification of an amino acid in the ATP binding site of Na+/K(+)-ATPase after photochemical labeling with 8-azido-ATP.

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Importance of Na,K-ATPase residue alpha 1-Arg544 in the segment Arg544-Asp567 for high-affinity binding of ATP, ADP, or MgATP.

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Phe(475) and Glu(446) but not Ser(445) participate in ATP-binding to the alpha-subunit of Na(+)/K(+)-ATPase

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Functional role of "N" (nucleotide) and "P" (phosphorylation) domain interactions in the sarcoplasmic reticulum (SERCA) ATPase

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Cloning, expression, purification and crystallization of the N-domain from the alpha(2) subunit of the membrane-spanning Na,K-ATPase protein

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