The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.
Crystal structure of the sodium-potassium pump (Na+,K+-ATPase) with bound potassium and ouabain
Open accessAbstract
The sodium-potassium pump (Na+,K+-ATPase) is responsible for establishing Na+and K+concentration gradients across the plasma membrane and therefore plays an essential role in, for instance, generating action potentials. Cardiac glycosides, prescribed for congestive heart failure for more than 2 centuries, are efficient inhibitors of this ATPase. Here we describe a crystal structure of Na+,K+-ATPase with bound ouabain, a representative cardiac glycoside, at 2.8 Å resolution in a state analogous to E2·2K+·Pi. Ouabain is deeply inserted into the transmembrane domain with the lactone ring very close to the bound K+, in marked contrast to previous models. Due to antagonism between ouabain and K+, the structure represents a low-affinity ouabain-bound state. Yet, most of the mutagenesis data obtained with the high-affinity state are readily explained by the present crystal structure, indicating that the binding site for ouabain is essentially the same. According to a homology model for the high affinity state, it is a closure of the binding cavity that confers a high affinity.
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Metadata
- Authors
- Ogawa, H., Shinoda, T., Cornelius, F., & Toyoshima, C.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2009-08-18
- Volume
- 106
- Issue
- 33
- Pages
- 13742-13747
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2083448771
- Cited by
- 326
- References
- 24
- FWCI
- 9.24
- Type
- journal article
- Language
- en
- Open access
- green
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- Ogawa, H., Shinoda, T., Cornelius, F., & Toyoshima, C. (2009). Crystal structure of the sodium-potassium pump (Na+,K+-ATPase) with bound potassium and ouabain. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0907054106
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