| First Author | Nishida M | Year | 2002 |
| Journal | Cell | Volume | 111 |
| Issue | 7 | Pages | 957-65 |
| PubMed ID | 12507423 | Mgi Jnum | J:80991 |
| Mgi Id | MGI:2447925 | Doi | 10.1016/s0092-8674(02)01227-8 |
| Citation | Nishida M, et al. (2002) Structural Basis of Inward Rectification. Cytoplasmic Pore of the G Protein-Gated Inward Rectifier GIRK1 at 1.8 A Resolution. Cell 111(7):957-65 |
| abstractText | Inward rectifier K(+) channels govern the resting membrane voltage in many cells. Regulation of these ion channels via G protein-coupled receptor signaling underlies the control of heart rate and the actions of neurotransmitters in the central nervous system. We have determined the protein structure formed by the intracellular N- and C termini of the G protein-gated inward rectifier K(+) channel GIRK1 at 1.8 A resolution. A cytoplasmic pore, conserved among inward rectifier K(+) channels, extends the ion pathway to 60 A, nearly twice the length of a canonical transmembrane K(+) channel. The cytoplasmic pore is lined by acidic and hydrophobic amino acids, creating a favorable environment for polyamines, which block the pore. These results explain in structural and chemical terms the basis of inward rectification, and they also have implications for G protein regulation of GIRK channels. |
