3SYQ

Crystal structure of the G protein-gated inward rectifier K+ channel GIRK2 (Kir3.2) R201A mutant in complex with PIP2

Summary for 3SYQ

• Entry DOI: 10.2210/pdb3syq/pdb
• Related: 3SYA 3SYC 3SYO 3SYP
• Descriptor: G protein-activated inward rectifier potassium channel 2, [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate, POTASSIUM ION (3 entities in total)
• Functional Keywords: ion channel, potassium channel, inward rectification, sodium binding, pip2 binding, g protein binding, metal transport
• Biological source: Mus musculus (mouse)
• Cellular location: Membrane; Multi-pass membrane protein: P48542
• Total number of polymer chains: 2
• Total formula weight: 78854.65

Authors

Whorton, M.R.,MacKinnon, R. (deposition date: 2011-07-18, release date: 2011-10-12, Last modification date: 2024-11-06)

Primary citation

Whorton, M.R.,Mackinnon, R.
Crystal Structure of the Mammalian GIRK2 K(+) Channel and Gating Regulation by G Proteins, PIP(2), and Sodium.
Cell(Cambridge,Mass.), 147:199-208, 2011

PubMed Abstract: 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 PIP(2) suggest that G proteins open only the G loop gate in the absence of PIP(2), but in the presence of PIP(2) 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 structural basis for understanding multiligand regulation of GIRK channel gating.

PubMed: 21962516
DOI: 10.1016/j.cell.2011.07.046

Experimental method

X-RAY DIFFRACTION (3.44 Å)