The DOI matches its Crossref record; 55 of the 55 references it cites were found in a registry or an index.
Crystal Structure of the Mammalian GIRK2 K+ Channel and Gating Regulation by G Proteins, PIP2, and Sodium
Open accessAbstract
Summary G-protein-gated K+ channels (Kir3.1–Kir3.4) control electrical excitability in many different cells. Among their functions relevant to human physiology and disease, they regulate the heart rate and govern a wide range of neuronal activities. Here we present the first crystal structures of a G-protein-gated K+ channel. By comparing the wild-type structure to that of a constitutively active mutant, we identify a global conformational change through which G-proteins could open a G-loop gate in the cytoplasmic domain. The structures of both channels in the absence and presence of PIP2 show that G-proteins open only the G-loop gate in the absence of PIP2, but in the presence of PIP2 the G-loop gate and a second inner helix gate become coupled, so that both gates open. We also identify a strategically located Na+ ion-binding site, which would allow intracellular Na+ to modulate GIRK channel activity. These data provide a mechanistic description of multi-ligand regulation of GIRK channel gating.
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Metadata
- Authors
- Whorton, M. R., & MacKinnon, R.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2011-09
- Volume
- 147
- Issue
- 1
- Pages
- 199-208
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2007061409
- Cited by
- 441
- References
- 55
- FWCI
- 14.93
- Type
- journal article
- Language
- en
- Open access
- bronze
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